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Article ; Online: ATP-Dependent Steps in Peroxisomal Protein Import.

Platta, Harald W / Jeske, Julia / Schmidt, Nadine / Erdmann, Ralf

2024

Abstract: Peroxisomes are organelles that play a central role in lipid metabolism and cellular redox homeostasis. The import of peroxisomal matrix proteins by peroxisomal targeting signal (PTS) receptors is an ATP-dependent mechanism. However, the energy-dependent ...

Abstract	Peroxisomes are organelles that play a central role in lipid metabolism and cellular redox homeostasis. The import of peroxisomal matrix proteins by peroxisomal targeting signal (PTS) receptors is an ATP-dependent mechanism. However, the energy-dependent steps do not occur early during the binding of the receptor-cargo complex to the membrane but late, because they are linked to the peroxisomal export complex for the release of the unloaded receptor. The first ATP-demanding step is the cysteine-dependent monoubiquitination of the PTS receptors, which is required for recognition by the AAA+ peroxins. They execute the second ATP-dependent step by extracting the ubiqitinated PTS receptors from the membrane for release back to the cytosol. After deubiquitination, the PTS receptors regain import competence and can facilitate further rounds of cargo import. Here, we give a general overview and discuss recent data regarding the ATP-dependent steps in peroxisome protein import.
Language	English
Publishing date	2024-04-15
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	207924-0
ISSN	1545-4509 ; 0066-4154
ISSN (online)	1545-4509
ISSN	0066-4154
DOI	10.1146/annurev-biochem-030222-111227
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Article ; Online: The ides of MARCH5: The E3 ligase essential for peroxisome degradation by pexophagy.

Platta, Harald W / Erdmann, Ralf

The Journal of cell biology

2021 Volume 221, Issue 1

Abstract: A recent study by Zheng et al. (2021. J. Cell Biol.https://doi.org/10.1083/jcb.202103156) identifies the ubiquitin-protein ligase (E3) MARCH5 as a dual-organelle localized protein that not only targets to mitochondria but also to peroxisomes in a PEX19- ... ...

Abstract	A recent study by Zheng et al. (2021. J. Cell Biol.https://doi.org/10.1083/jcb.202103156) identifies the ubiquitin-protein ligase (E3) MARCH5 as a dual-organelle localized protein that not only targets to mitochondria but also to peroxisomes in a PEX19-mediated manner. Moreover, the authors demonstrate that the Torin1-dependent induction of pexophagy is executed by the MARCH5-catalyzed ubiquitination of the peroxisomal membrane protein PMP70.
MeSH term(s)	Macroautophagy ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Peroxisomes/metabolism ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination
Chemical Substances	Membrane Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2021-12-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202111008
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Article ; Online: Autophagy Stimulus-Dependent Role of the Small GTPase Ras2 in Peroxisome Degradation.

Boutouja, Fahd / Platta, Harald W

Biomolecules

2020 Volume 10, Issue 11

Abstract: The changing accessibility of nutrient resources induces the reprogramming of cellular metabolism in order to adapt the cell to the altered growth conditions. The nutrient-depending signaling depends on the kinases mTOR (mechanistic target of rapamycin), ...

Abstract	The changing accessibility of nutrient resources induces the reprogramming of cellular metabolism in order to adapt the cell to the altered growth conditions. The nutrient-depending signaling depends on the kinases mTOR (mechanistic target of rapamycin), which is mainly activated by nitrogen-resources, and PKA (protein kinase A), which is mainly activated by glucose, as well as both of their associated factors. These systems promote protein synthesis and cell proliferation, while they inhibit degradation of cellular content by unselective bulk autophagy. Much less is known about their role in selective autophagy pathways, which have a more regulated cellular function. Especially, we were interested to analyse the central Ras2-module of the PKA-pathway in the context of peroxisome degradation. Yeast Ras2 is homologous to the mammalian Ras proteins, whose mutant forms are responsible for 33% of human cancers. In the present study, we were able to demonstrate a context-dependent role of Ras2 activity depending on the type of mTOR-inhibition and glucose-sensing situation. When mTOR was inhibited directly via the macrolide rapamycin, peroxisome degradation was still partially suppressed by Ras2, while inactivation of Ras2 resulted in an enhanced degradation of peroxisomes, suggesting a role of Ras2 in the inhibition of peroxisome degradation in glucose-grown cells. In contrast, the inhibition of mTOR by shifting cells from oleate-medium, which lacks glucose, to pexophagy-medium, which contains glucose and is limited in nitrogen, required Ras2-activity for efficient pexophagy, strongly suggesting that the role of Ras2 in glucose sensing-associated signaling is more important in this context than its co-function in mTOR-related autophagy-inhibition.
MeSH term(s)	Autophagy/physiology ; Glucose/metabolism ; Peroxisomes/metabolism ; Peroxisomes/pathology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; ras Proteins/genetics ; ras Proteins/metabolism
Chemical Substances	Saccharomyces cerevisiae Proteins ; RAS2 protein, S cerevisiae (EC 3.6.5.2) ; ras Proteins (EC 3.6.5.2) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2020-11-14
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom10111553
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Article ; Online: The novel peroxin Pex37: the Pxmp2 family joins the peroxisomal fission machinery.

Platta, Harald W / Erdmann, Ralf

The FEBS journal

2019 Volume 287, Issue 9, Page(s) 1737–1741

Abstract: Peroxisomes can undergo fission during cell division, followed by their segregation between mother and daughter cells. Despite species-specific variations in the molecular composition of the fission machinery, the central mechanistic factors can be ... ...

Abstract	Peroxisomes can undergo fission during cell division, followed by their segregation between mother and daughter cells. Despite species-specific variations in the molecular composition of the fission machinery, the central mechanistic factors can be assigned to two groups: the Pex11 family and the dynamin-related protein family. In a recent study, Singh et al. describe the involvement of a member of the Pxmp2-related protein family in peroxisome fission: the novel peroxin Pex37.
MeSH term(s)	Intracellular Membranes ; Peroxins ; Peroxisomes ; Proteins ; Saccharomycetales
Chemical Substances	Peroxins ; Proteins
Language	English
Publishing date	2019-12-20
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.15153
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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
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Article: mTOR: A Cellular Regulator Interface in Health and Disease.

Boutouja, Fahd / Stiehm, Christian M / Platta, Harald W

Cells

2019 Volume 8, Issue 1

Abstract: The mechanistic target of Rapamycin (mTOR) is a ubiquitously-conserved serine/threonine kinase, which has a central function in integrating growth signals and orchestrating their physiologic effects on cellular level. mTOR is the core component of ... ...

Abstract	The mechanistic target of Rapamycin (mTOR) is a ubiquitously-conserved serine/threonine kinase, which has a central function in integrating growth signals and orchestrating their physiologic effects on cellular level. mTOR is the core component of differently composed signaling complexes that differ in protein composition and molecular targets. Newly identified classes of mTOR inhibitors are being developed to block autoimmune diseases and transplant rejections but also to treat obesity, diabetes, and different types of cancer. Therefore, the selective and context-dependent inhibition of mTOR activity itself might come into the focus as molecular target to prevent severe diseases and possibly to extend life span. This review provides a general introduction to the molecular composition and physiologic function of mTOR complexes as part of the Special Issue "2018 Select Papers by
MeSH term(s)	Aging/drug effects ; Aging/metabolism ; Animals ; Autoimmune Diseases/drug therapy ; Autoimmune Diseases/metabolism ; Diabetes Mellitus/drug therapy ; Diabetes Mellitus/metabolism ; Humans ; Mechanistic Target of Rapamycin Complex 1/antagonists & inhibitors ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Mechanistic Target of Rapamycin Complex 2/antagonists & inhibitors ; Mechanistic Target of Rapamycin Complex 2/metabolism ; Neoplasms/drug therapy ; Neoplasms/metabolism ; Obesity/drug therapy ; Obesity/metabolism ; Signal Transduction ; TOR Serine-Threonine Kinases/antagonists & inhibitors ; TOR Serine-Threonine Kinases/physiology
Chemical Substances	TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Mechanistic Target of Rapamycin Complex 2 (EC 2.7.11.1)
Language	English
Publishing date	2019-01-02
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2661518-6
ISSN	2073-4409
ISSN	2073-4409
DOI	10.3390/cells8010018
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Article ; Online: The Peroxisomal PTS1-Import Defect of PEX1 - Deficient Cells Is Independent of Pexophagy in Saccharomyces cerevisiae

Thomas Mastalski / Rebecca Brinkmeier / Harald W. Platta

International Journal of Molecular Sciences, Vol 21, Iss 3, p

2020 Volume 867

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 PEX1 deletion-induced pexophagy does not restore peroxisomal matrix protein import or the peroxisomal function in beta-oxidation in yeast. Therefore, we conclude that Pex1 is directly and essentially involved in peroxisomal matrix protein import, and that the PEX1 deletion-induced pexophagy is not responsible for the defect in peroxisomal function. In order to point out the conserved mechanism, we discuss our findings in the context of the working models of peroxisomal biogenesis and pexophagy in yeasts and mammals.
Keywords	atg36 ; pex1 ; pexophagy ; peroxisomal protein import ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	570
Language	English
Publishing date	2020-01-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Book ; Online ; Thesis: Funktionelle Charakterisierung ATP- und GTP-abhängiger Schritte der Pexophagie in Saccharomyces cerevisiae

Boutouja, Fahd [Verfasser] / Platta, Harald W. [Gutachter] / Wiese, Stefan [Gutachter]

2020

Author's details	Fahd Boutouja ; Gutachter: Harald W. Platta, Stefan Wiese ; Fakultät für Biologie und Biotechnologie
Keywords	Biowissenschaften, Biologie ; Life Science, Biology
Subject code	sg570
Language	German
Publisher	Ruhr-Universität Bochum
Publishing place	Bochum
Document type	Book ; Online ; Thesis
Database	Digital theses on the web

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Article ; Online: mTOR

Fahd Boutouja / Christian M. Stiehm / Harald W. Platta

Cells, Vol 8, Iss 1, p

A Cellular Regulator Interface in Health and Disease

2019 Volume 18

Abstract	The mechanistic target of Rapamycin (mTOR) is a ubiquitously-conserved serine/threonine kinase, which has a central function in integrating growth signals and orchestrating their physiologic effects on cellular level. mTOR is the core component of differently composed signaling complexes that differ in protein composition and molecular targets. Newly identified classes of mTOR inhibitors are being developed to block autoimmune diseases and transplant rejections but also to treat obesity, diabetes, and different types of cancer. Therefore, the selective and context-dependent inhibition of mTOR activity itself might come into the focus as molecular target to prevent severe diseases and possibly to extend life span. This review provides a general introduction to the molecular composition and physiologic function of mTOR complexes as part of the Special Issue “2018 Select Papers by Cells’ Editorial Board Members”.
Keywords	mTOR ; autophagy ; kinase ; phosphorylation ; aging ; cancer ; Biology (General) ; QH301-705.5
Language	English
Publishing date	2019-01-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: The class III phosphatidylinositol 3-kinase Vps34 in Saccharomyces cerevisiae.

Reidick, Christina / Boutouja, Fahd / Platta, Harald W

Biological chemistry

2017 Volume 398, Issue 5-6, Page(s) 677–685

Abstract: The class III phosphatidylinositol 3-kinase Vps34 (vacuolar protein sorting 34) catalyzes for the formation of the signaling lipid phosphatidylinositol-3-phopsphate, which is a central factor in the regulation of autophagy, endocytic trafficking and ... ...

Abstract	The class III phosphatidylinositol 3-kinase Vps34 (vacuolar protein sorting 34) catalyzes for the formation of the signaling lipid phosphatidylinositol-3-phopsphate, which is a central factor in the regulation of autophagy, endocytic trafficking and vesicular transport. In this article, we discuss the functional role of the lipid kinase Vps34 in Saccharomyces cerevisiae.
MeSH term(s)	Animals ; Class III Phosphatidylinositol 3-Kinases/chemistry ; Class III Phosphatidylinositol 3-Kinases/metabolism ; GTP-Binding Proteins/metabolism ; Humans ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; Saccharomyces cerevisiae/enzymology ; Signal Transduction
Chemical Substances	Protein Subunits ; Class III Phosphatidylinositol 3-Kinases (EC 2.7.1.137) ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2017-05-01
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	1334659-3
ISSN	1437-4315 ; 1431-6730 ; 1432-0355
ISSN (online)	1437-4315
ISSN	1431-6730 ; 1432-0355
DOI	10.1515/hsz-2016-0288
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