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Article ; Online: Peroxisome population control by phosphoinositide signaling at the endoplasmic reticulum-plasma membrane interface.

Knoblach, Barbara / Rachubinski, Richard A

2023 Volume 25, Issue 1, Page(s) e12923

Abstract: Phosphoinositides are lipid signaling molecules acting at the interface of membranes and the cytosol to regulate membrane trafficking, lipid transport and responses to extracellular stimuli. Peroxisomes are multicopy organelles that are highly responsive ...

Abstract	Phosphoinositides are lipid signaling molecules acting at the interface of membranes and the cytosol to regulate membrane trafficking, lipid transport and responses to extracellular stimuli. Peroxisomes are multicopy organelles that are highly responsive to changes in metabolic and environmental conditions. In yeast, peroxisomes are tethered to the cell cortex at defined focal structures containing the peroxisome inheritance protein, Inp1p. We investigated the potential impact of changes in cortical phosphoinositide levels on the peroxisome compartment of the yeast cell. Here we show that the phosphoinositide, phosphatidylinositol-4-phosphate (PI4P), found at the junction of the cortical endoplasmic reticulum and plasma membrane (cER-PM) acts to regulate the cell's peroxisome population. In cells lacking a cER-PM tether or the enzymatic activity of the lipid phosphatase Sac1p, cortical PI4P is elevated, peroxisome numbers and motility are increased, and peroxisomes are no longer firmly tethered to Inp1p-containing foci. Reattachment of the cER to the PM through an artificial ER-PM "staple" in cells lacking the cER-PM tether does not restore peroxisome populations to the wild-type condition, demonstrating that integrity of PI4P signaling at the cell cortex is required for peroxisome homeostasis.
MeSH term(s)	Phosphatidylinositols/metabolism ; Peroxisomes/metabolism ; Saccharomyces cerevisiae/metabolism ; Membrane Proteins/metabolism ; Population Control ; Endoplasmic Reticulum/metabolism ; Cell Membrane/metabolism
Chemical Substances	Phosphatidylinositols ; Membrane Proteins
Language	English
Publishing date	2023-11-05
Publishing country	England
Document type	Journal Article
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1111/tra.12923
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Article ; Online: Determinants of the assembly, integrity and maintenance of the endoplasmic reticulum-peroxisome tether.

Knoblach, Barbara / Rachubinski, Richard A

Traffic (Copenhagen, Denmark)

2019 Volume 20, Issue 3, Page(s) 213–225

Abstract: Organelle tethering and intercommunication are crucial for proper cell function. We previously described a tether between peroxisomes and the endoplasmic reticulum (ER) that acts in peroxisome population control in the yeast, Saccharomyces cerevisiae. ... ...

Abstract	Organelle tethering and intercommunication are crucial for proper cell function. We previously described a tether between peroxisomes and the endoplasmic reticulum (ER) that acts in peroxisome population control in the yeast, Saccharomyces cerevisiae. Components of this tether are Pex3p, an integral membrane protein of both peroxisomes and the ER and Inp1p, a connector that links peroxisomes to the ER. Here, we report the analysis of random Inp1p mutants that enabled identification of regions in Inp1p required for the assembly and maintenance of the ER-peroxisome tether. Interaction analysis between Inp1p mutants and known Inp1p-binding proteins demonstrated that Pex3p and Inp1p do not constitute the sole components of the ER-peroxisome tether. Deletion of these Inp1p interactors whose steady-state localization is outside of ER-peroxisome tethers affected peroxisome dynamics. Our findings are consistent with the presence of regulatory cues that act on ER-peroxisome tethers and point to the existence of membrane contact sites between peroxisomes and organelles other than the ER.
MeSH term(s)	Endoplasmic Reticulum/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Peroxins/genetics ; Peroxins/metabolism ; Peroxisomes/metabolism ; Protein Binding ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	INP1 protein, S cerevisiae ; Membrane Proteins ; PEX3 protein, S cerevisiae ; Peroxins ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2019-01-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1111/tra.12635
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Article ; Online: Reconstitution of human peroxisomal β-oxidation in yeast.

Knoblach, Barbara / Rachubinski, Richard A

FEMS yeast research

2018 Volume 18, Issue 8

Abstract: We report the permanent introduction of the human peroxisomal β-oxidation enzymatic machinery required for straight chain degradation of fatty acids into the yeast, Saccharomyces cerevisiae. Peroxisomal β-oxidation encompasses four sequential reactions ... ...

Abstract	We report the permanent introduction of the human peroxisomal β-oxidation enzymatic machinery required for straight chain degradation of fatty acids into the yeast, Saccharomyces cerevisiae. Peroxisomal β-oxidation encompasses four sequential reactions that are confined to three enzymes. The genes encoding human acyl-CoA oxidase 1, peroxisomal multifunctional enzyme type 2 and 3-ketoacyl-CoA thiolase were introduced into the genomic loci of their yeast gene equivalents. The human β-oxidation genes were individually tagged with sequence coding for GFP and expression of the protein chimeras as well as their targeting to peroxisomes was confirmed. Functional complementation of the β-oxidation pathway was assessed by growth on media containing fatty acids of different chain lengths. Yeast cells exhibited distinctive substrate specificities depending on whether they expressed the human or their endogenous β-oxidation machinery. The genetic engineering of yeast to contain a 'humanized' organelle is a first step for the in vivo study of human peroxisome disorders in a model organism.
MeSH term(s)	Fatty Acids/metabolism ; Genetic Complementation Test ; Humans ; Organisms, Genetically Modified/enzymology ; Organisms, Genetically Modified/genetics ; Organisms, Genetically Modified/metabolism ; Oxidation-Reduction ; Peroxisomes/enzymology ; Peroxisomes/genetics ; Peroxisomes/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism
Chemical Substances	Fatty Acids ; Recombinant Proteins
Language	English
Publishing date	2018-08-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2036775-2
ISSN	1567-1364 ; 1567-1356
ISSN (online)	1567-1364
ISSN	1567-1356
DOI	10.1093/femsyr/foy092
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Article ; Online: Peroxisomes exhibit compromised structure and matrix protein content in SARS-CoV-2-infected cells.

Knoblach, Barbara / Ishida, Ray / Hobman, Tom C / Rachubinski, Richard A

Molecular biology of the cell

2021 Volume 32, Issue 14, Page(s) 1273–1282

Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a novel coronavirus that has triggered global health and economic crises. Here we report the effects of SARS-CoV-2 infection on peroxisomes of human cell lines Huh-7 and SK-N-SH. Peroxisomes ...

Abstract	Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a novel coronavirus that has triggered global health and economic crises. Here we report the effects of SARS-CoV-2 infection on peroxisomes of human cell lines Huh-7 and SK-N-SH. Peroxisomes undergo dramatic changes in morphology in SARS-CoV-2-infected cells. Rearrangement of peroxisomal membranes is followed by redistribution of peroxisomal matrix proteins to the cytosol, resulting in a dramatic decrease in the number of mature peroxisomes. The SARS-CoV-2 ORF14 protein was shown to interact physically with human PEX14, a peroxisomal membrane protein required for matrix protein import and peroxisome biogenesis. Given the important roles of peroxisomes in innate immunity, SARS-CoV-2 may directly target peroxisomes, resulting in loss of peroxisome structural integrity, matrix protein content and ability to function in antiviral signaling.
MeSH term(s)	Animals ; Cell Line ; Cell Membrane/pathology ; Chlorocebus aethiops ; Coronavirus Nucleocapsid Proteins/metabolism ; Extracellular Matrix Proteins/metabolism ; Humans ; Membrane Proteins/metabolism ; Peroxisomes/metabolism ; Peroxisomes/pathology ; Peroxisomes/virology ; Phosphoproteins/metabolism ; Repressor Proteins/metabolism ; SARS-CoV-2/metabolism ; Vero Cells
Chemical Substances	Coronavirus Nucleocapsid Proteins ; Extracellular Matrix Proteins ; Membrane Proteins ; PEX14 protein, human ; Phosphoproteins ; Repressor Proteins ; nucleocapsid phosphoprotein, SARS-CoV-2
Language	English
Publishing date	2021-05-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E21-02-0074
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Zs.A 2853: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article: Reconstitution of human peroxisomal β-oxidation in yeast

Knoblach, Barbara / Rachubinski, Richard A

FEMS yeast research. 2018 Aug. 17, v. 18, no. 8

2018

Abstract	We report the permanent introduction of the human peroxisomal β-oxidation enzymatic machinery required for straight chain degradation of fatty acids into the yeast, Saccharomyces cerevisiae. Peroxisomal β-oxidation encompasses four sequential reactions that are confined to three enzymes. The genes encoding human acyl-CoA oxidase 1, peroxisomal multifunctional enzyme type 2 and 3-ketoacyl-CoA thiolase were introduced into the genomic loci of their yeast gene equivalents. The human β-oxidation genes were individually tagged with sequence coding for GFP and expression of the protein chimeras as well as their targeting to peroxisomes was confirmed. Functional complementation of the β-oxidation pathway was assessed by growth on media containing fatty acids of different chain lengths. Yeast cells exhibited distinctive substrate specificities depending on whether they expressed the human or their endogenous β-oxidation machinery. The genetic engineering of yeast to contain a ‘humanized’ organelle is a first step for the in vivo study of human peroxisome disorders in a model organism.
Keywords	Saccharomyces cerevisiae ; acyl-CoA oxidase ; beta oxidation ; fatty acids ; genes ; genetic engineering ; genomics ; humans ; in vivo studies ; loci ; models ; peroxisomes ; substrate specificity ; yeasts
Language	English
Dates of publication	2018-0817
Publishing place	Oxford University Press
Document type	Article
ZDB-ID	2036775-2
ISSN	1567-1364 ; 1567-1356
ISSN (online)	1567-1364
ISSN	1567-1356
DOI	10.1093/femsyr/foy092
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Article ; Online: The early-acting glycosome biogenic protein Pex3 is essential for trypanosome viability.

Banerjee, Hiren / Knoblach, Barbara / Rachubinski, Richard A

Life science alliance

2019 Volume 2, Issue 4

Abstract: Trypanosomatid parasites are infectious agents for diseases such as African sleeping sickness, Chagas disease, and leishmaniasis that threaten millions of people, mostly in the emerging world. Trypanosomes compartmentalize glycolytic enzymes to an ... ...

Abstract	Trypanosomatid parasites are infectious agents for diseases such as African sleeping sickness, Chagas disease, and leishmaniasis that threaten millions of people, mostly in the emerging world. Trypanosomes compartmentalize glycolytic enzymes to an organelle called the glycosome, a specialized peroxisome. Functionally intact glycosomes are essential for trypanosomatid viability, making glycosomal proteins as potential drug targets against trypanosomatid diseases. Peroxins (Pex), of which Pex3 is the master regulator, control glycosome biogenesis. Although Pex3 has been found throughout the eukaryota, its identity has remained stubbornly elusive in trypanosomes. We used bioinformatics predictive of protein secondary structure to identify trypanosomal Pex3. Microscopic and biochemical analyses showed trypanosomal Pex3 to be glycosomal. Interaction of Pex3 with the peroxisomal membrane protein receptor Pex19 observed for other eukaryotes is replicated by trypanosomal Pex3 and Pex19. Depletion of Pex3 leads to mislocalization of glycosomal proteins to the cytosol, reduced glycosome numbers, and trypanosomatid death. Our findings are consistent with
MeSH term(s)	Gene Expression Regulation ; Genes, Essential ; Membrane Proteins/metabolism ; Microbial Viability ; Microbodies/metabolism ; Models, Molecular ; Peroxins/chemistry ; Peroxins/genetics ; Peroxins/metabolism ; Protein Structure, Secondary ; Structural Homology, Protein ; Trypanosoma/growth & development ; Trypanosoma/metabolism
Chemical Substances	Membrane Proteins ; Peroxins
Language	English
Publishing date	2019-07-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2575-1077
ISSN (online)	2575-1077
DOI	10.26508/lsa.201900421
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Article ; Online: How peroxisomes partition between cells. A story of yeast, mammals and filamentous fungi.

Knoblach, Barbara / Rachubinski, Richard A

Current opinion in cell biology

2016 Volume 41, Page(s) 73–80

Abstract: Eukaryotic cells are subcompartmentalized into discrete, membrane-enclosed organelles. These organelles must be preserved in cells over many generations to maintain the selective advantages afforded by compartmentalization. Cells use complex molecular ... ...

Abstract	Eukaryotic cells are subcompartmentalized into discrete, membrane-enclosed organelles. These organelles must be preserved in cells over many generations to maintain the selective advantages afforded by compartmentalization. Cells use complex molecular mechanisms of organelle inheritance to achieve high accuracy in the sharing of organelles between daughter cells. Here we focus on how a multi-copy organelle, the peroxisome, is partitioned in yeast, mammalian cells, and filamentous fungi, which differ in their mode of cell division. Cells achieve equidistribution of their peroxisomes through organelle transport and retention processes that act coordinately, although the strategies employed vary considerably by organism. Nevertheless, we propose that mechanisms common across species apply to the partitioning of all membrane-enclosed organelles.
MeSH term(s)	Animals ; Cell Compartmentation ; Fungi/cytology ; Fungi/metabolism ; Humans ; Mammals/metabolism ; Models, Biological ; Peroxisomes/metabolism ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/metabolism
Language	English
Publishing date	2016-08
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1026381-0
ISSN	1879-0410 ; 0955-0674
ISSN (online)	1879-0410
ISSN	0955-0674
DOI	10.1016/j.ceb.2016.04.004
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Article: Sharing with your children: Mechanisms of peroxisome inheritance.

Knoblach, Barbara / Rachubinski, Richard A

Biochimica et biophysica acta

2016 Volume 1863, Issue 5, Page(s) 1014–1018

Abstract: Organelle inheritance is the process by which eukaryotic cells actively replicate and equitably partition their organelles between mother cell and daughter cell at cytokinesis to maintain the benefits of subcellular compartmentalization. The budding ... ...

Abstract	Organelle inheritance is the process by which eukaryotic cells actively replicate and equitably partition their organelles between mother cell and daughter cell at cytokinesis to maintain the benefits of subcellular compartmentalization. The budding yeast Saccharomyces cerevisiae has proven invaluable in helping to define the factors involved in the inheritance of different organelles and in understanding how these factors act and interact to maintain balance in the organelle populations of actively dividing cells. Inheritance factors can be classified as motors that transport organelles, tethers that retain organelles, and connectors (receptors) that mediate the attachment of organelles to motors and anchors. This article will review how peroxisomes are inherited by cells, with a focus on budding yeast, and will discuss common themes and mechanisms of action that underlie the inheritance of all membrane-enclosed organelles.
MeSH term(s)	Biological Transport ; Cell Compartmentation ; Cytokinesis ; Eukaryotic Cells/metabolism ; Eukaryotic Cells/ultrastructure ; Gene Expression Regulation ; Humans ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Myosin Heavy Chains/genetics ; Myosin Heavy Chains/metabolism ; Myosin Type V/genetics ; Myosin Type V/metabolism ; Organelle Biogenesis ; Peroxins ; Peroxisomes/chemistry ; Peroxisomes/metabolism ; Receptors, Cytoplasmic and Nuclear/genetics ; Receptors, Cytoplasmic and Nuclear/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae/ultrastructure ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction
Chemical Substances	INP2 protein, S cerevisiae ; MYO2 protein, S cerevisiae ; Membrane Proteins ; PEX3 protein, S cerevisiae ; Peroxins ; Receptors, Cytoplasmic and Nuclear ; Saccharomyces cerevisiae Proteins ; Myosin Type V (EC 3.6.1.-) ; Myosin Heavy Chains (EC 3.6.4.1)
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.2015.11.023
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Article ; Online: Motors, anchors, and connectors: orchestrators of organelle inheritance.

Knoblach, Barbara / Rachubinski, Richard A

Annual review of cell and developmental biology

2015 Volume 31, Page(s) 55–81

Abstract: Organelle inheritance is a process whereby organelles are actively distributed between dividing cells at cytokinesis. Much valuable insight into the molecular mechanisms of organelle inheritance has come from the analysis of asymmetrically dividing cells, ...

Abstract	Organelle inheritance is a process whereby organelles are actively distributed between dividing cells at cytokinesis. Much valuable insight into the molecular mechanisms of organelle inheritance has come from the analysis of asymmetrically dividing cells, which transport a portion of their organelles to the bud while retaining another portion in the mother cell. Common principles apply to the inheritance of all organelles, although individual organelles use specific factors for their partitioning. Inheritance factors can be classified as motors, which are required for organelle transport; anchors, which immobilize organelles at distinct cell structures; or connectors, which mediate the attachment of organelles to motors and anchors. Here, we provide an overview of recent advances in the field of organelle inheritance and highlight how motor, anchor, and connector molecules choreograph the segregation of a multicopy organelle, the peroxisome. We also discuss the role of organelle population control in the generation of cellular diversity.
MeSH term(s)	Animals ; Biological Transport/physiology ; Cell Division/physiology ; Cytokinesis/physiology ; Humans ; Membrane Proteins ; Organelles/physiology ; Peroxisomes/physiology ; Saccharomyces cerevisiae/physiology
Chemical Substances	Membrane Proteins
Language	English
Publishing date	2015
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1293750-2
ISSN	1530-8995 ; 1081-0706
ISSN (online)	1530-8995
ISSN	1081-0706
DOI	10.1146/annurev-cellbio-100814-125553
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Article ; Online: Transport and retention mechanisms govern lipid droplet inheritance in Saccharomyces cerevisiae.

Knoblach, Barbara / Rachubinski, Richard A

Traffic (Copenhagen, Denmark)

2015 Volume 16, Issue 3, Page(s) 298–309

Abstract: Lipid droplets are ubiquitous cellular structures involved in energy homeostasis and metabolism that have long been considered as simple inert deposits of lipid. Here, we show that lipid droplets are bona fide organelles that are actively partitioned ... ...

Abstract	Lipid droplets are ubiquitous cellular structures involved in energy homeostasis and metabolism that have long been considered as simple inert deposits of lipid. Here, we show that lipid droplets are bona fide organelles that are actively partitioned between mother cell and daughter cell in Saccharomyces cerevisiae. Video microscopy revealed that a subset of lipid droplets moves from mother cell to bud in an ordered, vectorial process, while the remaining lipid droplets are retained by the mother cell. Bud-directed movement of lipid droplets is mediated by the molecular motor Myo2p, while retention of lipid droplets occurs at the perinuclear endoplasmic reticulum. Lipid droplets are thus apportioned between mother cell and daughter cell at cell division rather than being made anew.
MeSH term(s)	Biological Transport/physiology ; Cell Division/physiology ; Endoplasmic Reticulum/metabolism ; Endoplasmic Reticulum/physiology ; Homeostasis/physiology ; Lipid Droplets/physiology ; Lipids/physiology ; Myosin Heavy Chains/metabolism ; Myosin Type V/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae/physiology ; Saccharomyces cerevisiae Proteins/metabolism ; Stem Cells/metabolism ; Stem Cells/physiology
Chemical Substances	Lipids ; MYO2 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Myosin Type V (EC 3.6.1.-) ; Myosin Heavy Chains (EC 3.6.4.1)
Language	English
Publishing date	2015-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1111/tra.12247
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