LIVIVO - Search results -

Search results

Result 1 - 10 of total 11

Search options

Article ; Online: The Peroxisomal PTS1-Import Defect of

Mastalski, Thomas / Brinkmeier, Rebecca / Platta, Harald W

International journal of molecular sciences

2020 Volume 21, Issue 3

Abstract: The important physiologic role of peroxisomes is shown by the occurrence of peroxisomal biogenesis disorders (PBDs) in humans. This spectrum of autosomal recessive metabolic disorders is characterized by defective peroxisome assembly and impaired ... ...

Abstract	The important physiologic role of peroxisomes is shown by the occurrence of peroxisomal biogenesis disorders (PBDs) in humans. This spectrum of autosomal recessive metabolic disorders is characterized by defective peroxisome assembly and impaired peroxisomal functions. PBDs are caused by mutations in the peroxisomal biogenesis factors, which are required for the correct compartmentalization of peroxisomal matrix enzymes. Recent work from patient cells that contain the Pex1(G843D) point mutant suggested that the inhibition of the lysosome, and therefore the block of pexophagy, was beneficial for peroxisomal function. The resulting working model proposed that Pex1 may not be essential for matrix protein import at all, but rather for the prevention of pexophagy. Thus, the observed matrix protein import defect would not be caused by a lack of Pex1 activity, but rather by enhanced removal of peroxisomal membranes via pexophagy. In the present study, we can show that the specific block of
MeSH term(s)	ATPases Associated with Diverse Cellular Activities/deficiency ; ATPases Associated with Diverse Cellular Activities/genetics ; ATPases Associated with Diverse Cellular Activities/metabolism ; Macroautophagy ; Membrane Proteins/deficiency ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Peroxins/genetics ; Peroxins/metabolism ; Peroxisomal Targeting Signals/genetics ; Peroxisomes/metabolism ; Protein Transport ; Recombinant Fusion Proteins/biosynthesis ; Recombinant Fusion Proteins/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Membrane Proteins ; PEX11 protein, S cerevisiae ; Peroxins ; Peroxisomal Targeting Signals ; Recombinant Fusion Proteins ; Saccharomyces cerevisiae Proteins ; ATPases Associated with Diverse Cellular Activities (EC 3.6.4.-) ; PEX1 protein, S cerevisiae (EC 3.6.4.-)
Language	English
Publishing date	2020-01-29
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms21030867
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Article ; Online: Phosphorylation of the receptor protein Pex5p modulates import of proteins into peroxisomes.

Fischer, Sven / Bürgi, Jérôme / Gabay-Maskit, Shiran / Maier, Renate / Mastalski, Thomas / Yifrach, Eden / Obarska-Kosinska, Agnieszka / Rudowitz, Markus / Erdmann, Ralf / Platta, Harald W / Wilmanns, Matthias / Schuldiner, Maya / Zalckvar, Einat / Oeljeklaus, Silke / Drepper, Friedel / Warscheid, Bettina

Biological chemistry

2022 Volume 404, Issue 2-3, Page(s) 135–155

Abstract: Peroxisomes are organelles with vital functions in metabolism and their dysfunction is associated with human diseases. To fulfill their multiple roles, peroxisomes import nuclear-encoded matrix proteins, most carrying a peroxisomal targeting signal (PTS) ...

Abstract	Peroxisomes are organelles with vital functions in metabolism and their dysfunction is associated with human diseases. To fulfill their multiple roles, peroxisomes import nuclear-encoded matrix proteins, most carrying a peroxisomal targeting signal (PTS) 1. The receptor Pex5p recruits PTS1-proteins for import into peroxisomes; whether and how this process is posttranslationally regulated is unknown. Here, we identify 22 phosphorylation sites of Pex5p. Yeast cells expressing phospho-mimicking Pex5p-S507/523D (Pex5p
MeSH term(s)	Humans ; Phosphorylation ; Peroxisomes/metabolism ; Peroxisome-Targeting Signal 1 Receptor/metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism ; Carrier Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Protein Transport
Chemical Substances	Peroxisome-Targeting Signal 1 Receptor ; Receptors, Cytoplasmic and Nuclear ; Carrier Proteins
Language	English
Publishing date	2022-09-21
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1334659-3
ISSN	1437-4315 ; 1431-6730 ; 1432-0355
ISSN (online)	1437-4315
ISSN	1431-6730 ; 1432-0355
DOI	10.1515/hsz-2022-0168
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.50: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Vps10-mediated targeting of Pep4 determines the activity of the vacuole in a substrate-dependent manner.

Boutouja, Fahd / Stiehm, Christian M / Mastalski, Thomas / Brinkmeier, Rebecca / Reidick, Christina / El Magraoui, Fouzi / Platta, Harald W

Scientific reports

2019 Volume 9, Issue 1, Page(s) 10557

Abstract: The vacuole is the hydrolytic compartment of yeast cells and has a similar function as the lysosome of higher eukaryotes in detoxification and recycling of macromolecules. We analysed the contribution of single vacuolar enzymes to pexophagy and ... ...

Abstract	The vacuole is the hydrolytic compartment of yeast cells and has a similar function as the lysosome of higher eukaryotes in detoxification and recycling of macromolecules. We analysed the contribution of single vacuolar enzymes to pexophagy and identified the phospholipase Atg15, the V-ATPase factor Vma2 and the serine-protease Prb1 along with the already known aspartyl-protease Pep4 (Proteinase A) to be required for this pathway. We also analysed the trafficking receptor Vps10, which is required for an efficient vacuolar targeting of the precursor form of Pep4. Here we demonstrate a novel context-dependent role of Vps10 in autophagy. We show that reduced maturation of Pep4 in a VPS10-deletion strain affects the proteolytic activity of the vacuole depending on the type and amount of substrate. The VPS10-deletion has no effect on the degradation of the cytosolic protein Pgk1 via bulk autophagy or on the degradation of ribosomes via ribophagy. In contrast, the degradation of an excess of peroxisomes via pexophagy as well as mitochondria via mitophagy was significantly hampered in a VPS10-deletion strain and correlated with a decreased maturation level of Pep4. The results show that Vps10-mediated targeting of Pep4 limits the proteolytic capacity of the vacuole in a substrate-dependent manner.
MeSH term(s)	Aspartic Acid Endopeptidases/deficiency ; Aspartic Acid Endopeptidases/genetics ; Aspartic Acid Endopeptidases/metabolism ; Autophagy ; Gene Deletion ; Genes, Fungal ; Macroautophagy ; Models, Biological ; Peroxisomes/metabolism ; Phosphoglycerate Kinase/metabolism ; Proteolysis ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Substrate Specificity ; Vacuoles/metabolism ; Vesicular Transport Proteins/deficiency ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/metabolism
Chemical Substances	PEP1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Vesicular Transport Proteins ; Phosphoglycerate Kinase (EC 2.7.2.3) ; PEP4 protein, S cerevisiae (EC 3.4.23.) ; Aspartic Acid Endopeptidases (EC 3.4.23.-)
Language	English
Publishing date	2019-07-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-019-47184-7
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Vac8 Controls Vacuolar Membrane Dynamics during Different Autophagy Pathways in

Boutouja, Fahd / Stiehm, Christian M / Reidick, Christina / Mastalski, Thomas / Brinkmeier, Rebecca / Magraoui, Fouzi El / Platta, Harald W

Cells

2019 Volume 8, Issue 7

Abstract: The yeast vacuole is a vital organelle, which is required for the degradation of aberrant intracellular or extracellular substrates and the recycling of the resulting nutrients as newly available building blocks for the cellular metabolism. Like the ... ...

Abstract	The yeast vacuole is a vital organelle, which is required for the degradation of aberrant intracellular or extracellular substrates and the recycling of the resulting nutrients as newly available building blocks for the cellular metabolism. Like the plant vacuole or the mammalian lysosome, the yeast vacuole is the destination of biosynthetic trafficking pathways that transport the vacuolar enzymes required for its functions. Moreover, substrates destined for degradation, like extracellular endocytosed cargoes that are transported by endosomes/multivesicular bodies as well as intracellular substrates that are transported via different forms of autophagosomes, have the vacuole as destination. We found that non-selective bulk autophagy of cytosolic proteins as well as the selective autophagic degradation of peroxisomes (pexophagy) and ribosomes (ribophagy) was dependent on the armadillo repeat protein Vac8 in
MeSH term(s)	Autophagy ; Intracellular Membranes/metabolism ; Lipoylation ; Peroxisomes/metabolism ; Ribosomes/metabolism ; Saccharomyces cerevisiae/physiology ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Sequence Deletion ; Vacuoles/metabolism ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/metabolism
Chemical Substances	Saccharomyces cerevisiae Proteins ; VAC8 protein, S cerevisiae ; Vesicular Transport Proteins
Language	English
Publishing date	2019-06-30
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409
ISSN	2073-4409
DOI	10.3390/cells8070661
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Regulation of the Tumor-Suppressor BECLIN 1 by Distinct Ubiquitination Cascades.

Boutouja, Fahd / Brinkmeier, Rebecca / Mastalski, Thomas / El Magraoui, Fouzi / Platta, Harald W

International journal of molecular sciences

2017 Volume 18, Issue 12

Abstract: Autophagy contributes to cellular homeostasis through the degradation of various intracellular targets such as proteins, organelles and microbes. This relates autophagy to various diseases such as infections, neurodegenerative diseases and cancer. A ... ...

Abstract	Autophagy contributes to cellular homeostasis through the degradation of various intracellular targets such as proteins, organelles and microbes. This relates autophagy to various diseases such as infections, neurodegenerative diseases and cancer. A central component of the autophagy machinery is the class III phosphatidylinositol 3-kinase (PI3K-III) complex, which generates the signaling lipid phosphatidylinositol 3-phosphate (PtdIns3P). The catalytic subunit of this complex is the lipid-kinase VPS34, which associates with the membrane-targeting factor VPS15 as well as the multivalent adaptor protein BECLIN 1. A growing list of regulatory proteins binds to BECLIN 1 and modulates the activity of the PI3K-III complex. Here we discuss the regulation of BECLIN 1 by several different types of ubiquitination, resulting in distinct polyubiquitin chain linkages catalyzed by a set of E3 ligases. This contribution is part of the Special Issue "Ubiquitin System".
MeSH term(s)	Animals ; Beclin-1/genetics ; Beclin-1/metabolism ; Humans ; Phosphatidylinositol 3-Kinases/metabolism ; Signal Transduction ; Ubiquitination
Chemical Substances	Beclin-1 ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-)
Language	English
Publishing date	2017-11-27
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms18122541
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Regulation of peroxisome dynamics by phosphorylation.

Oeljeklaus, Silke / Schummer, Andreas / Mastalski, Thomas / Platta, Harald W / Warscheid, Bettina

Biochimica et biophysica acta

2016 Volume 1863, Issue 5, Page(s) 1027–1037

Abstract: Peroxisomes are highly dynamic organelles that can rapidly change in size, abundance, and protein content in response to alterations in nutritional and other environmental conditions. These dynamic changes in peroxisome features, referred to as ... ...

Abstract	Peroxisomes are highly dynamic organelles that can rapidly change in size, abundance, and protein content in response to alterations in nutritional and other environmental conditions. These dynamic changes in peroxisome features, referred to as peroxisome dynamics, rely on the coordinated action of several processes of peroxisome biogenesis. Revealing the regulatory mechanisms of peroxisome dynamics is an emerging theme in cell biology. These mechanisms are inevitably linked to and synchronized with the biogenesis and degradation of peroxisomes. To date, the key players and basic principles of virtually all steps in the peroxisomal life cycle are known, but regulatory mechanisms remained largely elusive. A number of recent studies put the spotlight on reversible protein phosphorylation for the control of peroxisome dynamics and highlighted peroxisomes as hubs for cellular signal integration and regulation. Here, we will present and discuss the results of several studies performed using yeast and mammalian cells that convey a sense of the impact protein phosphorylation may have on the modulation of peroxisome dynamics by regulating peroxisomal matrix and membrane protein import, proliferation, inheritance, and degradation. We further put forward the idea to make use of current data on phosphorylation sites of peroxisomal and peroxisome-associated proteins reported in advanced large-scale phosphoproteomic studies.
MeSH term(s)	Animals ; Autophagy ; Gene Expression Regulation ; Glycerol-3-Phosphate Dehydrogenase (NAD+)/genetics ; Glycerol-3-Phosphate Dehydrogenase (NAD+)/metabolism ; Humans ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Mice ; Organelle Biogenesis ; Peroxisomal Targeting Signal 2 Receptor ; Peroxisome-Targeting Signal 1 Receptor ; Peroxisomes/chemistry ; Peroxisomes/metabolism ; Phosphorylation ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Protein Transport ; Receptors, Cytoplasmic and Nuclear/genetics ; Receptors, Cytoplasmic and Nuclear/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction
Chemical Substances	INP2 protein, S cerevisiae ; Membrane Proteins ; Membrane Transport Proteins ; PEX5 protein, S cerevisiae ; PEX7 protein, S cerevisiae ; Peroxisomal Targeting Signal 2 Receptor ; Peroxisome-Targeting Signal 1 Receptor ; Protein Isoforms ; Receptors, Cytoplasmic and Nuclear ; Saccharomyces cerevisiae Proteins ; GPD1 protein, S cerevisiae (EC 1.1.1.8) ; Glycerol-3-Phosphate Dehydrogenase (NAD+) (EC 1.1.1.8)
Language	English
Publishing date	2016-05
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2015.12.022
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Uc I Zs.247: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: The deubiquitination of the PTS1-import receptor Pex5p is required for peroxisomal matrix protein import.

El Magraoui, Fouzi / Brinkmeier, Rebecca / Mastalski, Thomas / Hupperich, Alexander / Strehl, Christofer / Schwerter, Daniel / Girzalsky, Wolfgang / Meyer, Helmut E / Warscheid, Bettina / Erdmann, Ralf / Platta, Harald W

Biochimica et biophysica acta. Molecular cell research

2018 Volume 1866, Issue 2, Page(s) 199–213

Abstract: Peroxisomal biogenesis depends on the correct import of matrix proteins into the lumen of the organelle. Most peroxisomal matrix proteins harbor the peroxisomal targeting-type 1 (PTS1), which is recognized by the soluble PTS1-receptor Pex5p in the ... ...

Abstract	Peroxisomal biogenesis depends on the correct import of matrix proteins into the lumen of the organelle. Most peroxisomal matrix proteins harbor the peroxisomal targeting-type 1 (PTS1), which is recognized by the soluble PTS1-receptor Pex5p in the cytosol. Pex5p ferries the PTS1-proteins to the peroxisomal membrane and releases them into the lumen. Finally, the PTS1-receptor is monoubiquitinated on the conserved cysteine 6 in Saccharomyces cerevisiae. The monoubiquitinated Pex5p is recognized by the peroxisomal export machinery and is retrotranslocated into the cytosol for further rounds of protein import. However, the functional relevance of deubiquitination has not yet been addressed. In this study, we have analyzed a Pex5p-truncation lacking Cys6 [(Δ6)Pex5p], a construct with a ubiquitin-moiety genetically fused to the truncation [Ub-(Δ6)Pex5p], as well as a construct with a reduced susceptibility to deubiquitination [Ub(G75/76A)-(Δ6)Pex5p]. While the (Δ6)Pex5p-truncation is not functional, the Ub-(Δ6)Pex5p chimeric protein can facilitate matrix protein import. In contrast, the Ub(G75/76A)-(Δ6)Pex5p chimera exhibits a complete PTS1-import defect. The data show for the first time that not only ubiquitination but also deubiquitination rates are tightly regulated and that efficient deubiquitination of Pex5p is essential for peroxisomal biogenesis.
MeSH term(s)	Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Mutation/genetics ; Peroxins ; Peroxisomal Targeting Signals/physiology ; Peroxisome-Targeting Signal 1 Receptor/genetics ; Peroxisome-Targeting Signal 1 Receptor/metabolism ; Peroxisome-Targeting Signal 1 Receptor/physiology ; Peroxisomes/metabolism ; Peroxisomes/physiology ; Polyubiquitin/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Protein Processing, Post-Translational ; Protein Transport/physiology ; Proteolysis ; Receptors, Cytoplasmic and Nuclear/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Saccharomyces cerevisiae Proteins/physiology ; Sequence Deletion/genetics ; Signal Transduction ; Ubiquitin/metabolism ; Ubiquitination/physiology
Chemical Substances	Membrane Transport Proteins ; PEX5 protein, S cerevisiae ; Peroxins ; Peroxisomal Targeting Signals ; Peroxisome-Targeting Signal 1 Receptor ; Receptors, Cytoplasmic and Nuclear ; Saccharomyces cerevisiae Proteins ; Ubiquitin ; Polyubiquitin (120904-94-1) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2018-11-06
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2018.11.002
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Uc I Zs.247: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article: LMD proteomics provides evidence for hippocampus field-specific motor protein abundance changes with relevance to Alzheimer's disease.

Schrötter, Andreas / Oberhaus, Andrea / Kolbe, Katharina / Seger, Svenja / Mastalski, Thomas / El Magraoui, Fouzi / Hoffmann-Posorske, Edeltraut / Bohnert, Michael / Deckert, Jürgen / Braun, Christian / Graw, Matthias / Schmitz, Christoph / Arzberger, Thomas / Loosse, Christina / Heinsen, Helmut / Meyer, Helmut E / Müller, Thorsten

Biochimica et biophysica acta. Proteins and proteomics

2017 Volume 1865, Issue 6, Page(s) 703–714

Abstract: Background: Human hippocampal area Cornu Ammonis (CA) 1 is one of the first fields in the human telencephalon showing Alzheimer disease (AD)-specific neuropathological changes. In contrast, CA2 and CA3 are far later affected pointing to functional ... ...

Abstract	Background: Human hippocampal area Cornu Ammonis (CA) 1 is one of the first fields in the human telencephalon showing Alzheimer disease (AD)-specific neuropathological changes. In contrast, CA2 and CA3 are far later affected pointing to functional differences, which may be accompanied by differences in proteome endowment and changes. Methods: Human pyramidal cell layers of hippocampal areas CA1, CA2, and CA3 from neurologically unaffected individuals were excised using laser microdissection. The proteome of each individual sample was analyzed and differentially abundant proteins were validated by immuno-histochemistry. Results: Comparison of CA1 to CA2 revealed 223, CA1 to CA3 197 proteins with differential abundance, among them we found motor proteins MYO5A and DYNC1H1. Extension of the study to human hippocampus slices from AD patients revealed extensive depletion of these proteins in CA1 area compared to unaffected controls. Conclusion: High abundance of motor proteins in pyramidal cell layers CA1 compared to CA2 and CA3 points the specific vulnerability of this hippocampal area to transport-associated changes based on microtubule dysfunction and destabilization in AD.
MeSH term(s)	Aged ; Aged, 80 and over ; Alzheimer Disease/metabolism ; Chromatography, Liquid ; Female ; Hippocampus/metabolism ; Humans ; Immunohistochemistry ; Male ; Middle Aged ; Nerve Tissue Proteins/metabolism ; Proteomics ; Tandem Mass Spectrometry
Chemical Substances	Nerve Tissue Proteins
Language	English
Publishing date	2017-04-02
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 1570-9639 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	1570-9639 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbapap.2017.03.013
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Uc I Zs.247: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: The cytosolic domain of Pex22p stimulates the Pex4p-dependent ubiquitination of the PTS1-receptor.

El Magraoui, Fouzi / Schrötter, Andreas / Brinkmeier, Rebecca / Kunst, Lena / Mastalski, Thomas / Müller, Thorsten / Marcus, Katrin / Meyer, Helmut E / Girzalsky, Wolfgang / Erdmann, Ralf / Platta, Harald W

PloS one

2014 Volume 9, Issue 8, Page(s) e105894

Abstract: Peroxisomal biogenesis is an ubiquitin-dependent process because the receptors required for the import of peroxisomal matrix proteins are controlled via their ubiquitination status. A key step is the monoubiquitination of the import receptor Pex5p by the ...

Abstract	Peroxisomal biogenesis is an ubiquitin-dependent process because the receptors required for the import of peroxisomal matrix proteins are controlled via their ubiquitination status. A key step is the monoubiquitination of the import receptor Pex5p by the ubiquitin-conjugating enzyme (E2) Pex4p. This monoubiquitination is supposed to take place after Pex5p has released the cargo into the peroxisomal matrix and primes Pex5p for the extraction from the membrane by the mechano-enzymes Pex1p/Pex6p. These two AAA-type ATPases export Pex5p back to the cytosol for further rounds of matrix protein import. Recently, it has been reported that the soluble Pex4p requires the interaction to its peroxisomal membrane-anchor Pex22p to display full activity. Here we demonstrate that the soluble C-terminal domain of Pex22p harbours its biological activity and that this activity is independent from its function as membrane-anchor of Pex4p. We show that Pex4p can be functionally fused to the trans-membrane segment of the membrane protein Pex3p, which is not directly involved in Pex5p-ubiquitination and matrix protein import. However, this Pex3(N)-Pex4p chimera can only complement the double-deletion strain pex4Δ/pex22Δ and ensure optimal Pex5p-ubiquitination when the C-terminal part of Pex22p is additionally expressed in the cell. Thus, while the membrane-bound portion Pex22(N)p is not required when Pex4p is fused to Pex3(N)p, the soluble Pex22(C)p is essential for peroxisomal biogenesis and efficient monoubiquitination of the import receptor Pex5p by the E3-ligase Pex12p in vivo and in vitro. The results merge into a picture of an ubiquitin-conjugating complex at the peroxisomal membrane consisting of three domains: the ubiquitin-conjugating domain (Pex4p), a membrane-anchor domain (Pex22(N)p) and an enhancing domain (Pex22(C)p), with the membrane-anchor domain being mutually exchangeable, while the Ubc- and enhancer-domains are essential.
MeSH term(s)	ATPases Associated with Diverse Cellular Activities ; Adenosine Triphosphatases/genetics ; Adenosine Triphosphatases/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Deletion ; Gene Expression Regulation, Fungal ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Peroxins ; Peroxisome-Targeting Signal 1 Receptor ; Peroxisomes/metabolism ; Phosphorylation ; Protein Structure, Tertiary ; Protein Transport ; Receptors, Cytoplasmic and Nuclear/genetics ; Receptors, Cytoplasmic and Nuclear/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction ; Ubiquitin/genetics ; Ubiquitin/metabolism ; Ubiquitination
Chemical Substances	Membrane Proteins ; PEX3 protein, S cerevisiae ; PEX4 protein, S cerevisiae ; Peroxins ; Peroxisome-Targeting Signal 1 Receptor ; Pex22 protein, S cerevisiae ; Receptors, Cytoplasmic and Nuclear ; Recombinant Proteins ; Saccharomyces cerevisiae Proteins ; Ubiquitin ; Adenosine Triphosphatases (EC 3.6.1.-) ; ATPases Associated with Diverse Cellular Activities (EC 3.6.4.-) ; PEX1 protein, S cerevisiae (EC 3.6.4.-) ; PEX6 protein, S cerevisiae (EC 3.6.4.-)
Language	English
Publishing date	2014-08-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0105894
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: FE65 regulates and interacts with the Bloom syndrome protein in dynamic nuclear spheres - potential relevance to Alzheimer's disease.

Schrötter, Andreas / Mastalski, Thomas / Nensa, Fabian M / Neumann, Martin / Loosse, Christina / Pfeiffer, Kathy / Magraoui, Fouzi El / Platta, Harald W / Erdmann, Ralf / Theiss, Carsten / Uszkoreit, Julian / Eisenacher, Martin / Meyer, Helmut E / Marcus, Katrin / Müller, Thorsten

Journal of cell science

2013 Volume 126, Issue Pt 11, Page(s) 2480–2492

Abstract: The intracellular domain of the amyloid precursor protein (AICD) is generated following cleavage of the precursor by the γ-secretase complex and is involved in membrane to nucleus signaling, for which the binding of AICD to the adapter protein FE65 is ... ...

Abstract	The intracellular domain of the amyloid precursor protein (AICD) is generated following cleavage of the precursor by the γ-secretase complex and is involved in membrane to nucleus signaling, for which the binding of AICD to the adapter protein FE65 is essential. Here we show that FE65 knockdown causes a downregulation of the protein Bloom syndrome protein (BLM) and the minichromosome maintenance (MCM) protein family and that elevated nuclear levels of FE65 result in stabilization of the BLM protein in nuclear mobile spheres. These spheres are able to grow and fuse, and potentially correspond to the nuclear domain 10. BLM plays a role in DNA replication and repair mechanisms and FE65 was also shown to play a role in DNA damage response in the cell. A set of proliferation assays in our work revealed that FE65 knockdown in HEK293T cells reduced cell replication. On the basis of these results, we hypothesize that nuclear FE65 levels (nuclear FE65/BLM containing spheres) may regulate cell cycle re-entry in neurons as a result of increased interaction of FE65 with BLM and/or an increase in MCM protein levels. Thus, FE65 interactions with BLM and MCM proteins may contribute to the neuronal cell cycle re-entry observed in brains affected by Alzheimer's disease.
MeSH term(s)	Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Brain/metabolism ; Brain/pathology ; Cell Cycle ; Cell Line ; Cell Nucleus/genetics ; Cell Nucleus/metabolism ; Gene Knockdown Techniques ; Humans ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Neurons/metabolism ; Neurons/pathology ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; RecQ Helicases/genetics ; RecQ Helicases/metabolism
Chemical Substances	APBB1 protein, human ; APP protein, human ; Amyloid beta-Protein Precursor ; Nerve Tissue Proteins ; Nuclear Proteins ; Bloom syndrome protein (EC 3.6.1.-) ; RecQ Helicases (EC 3.6.4.12)
Language	English
Publishing date	2013-06-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.121004
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 1200: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 14: Show issues

Order via subito

Details ▾

To top

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito