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The dynamin-related protein Vps1 and the peroxisomal membrane protein Pex27 function together during peroxisome fission.
- Source :
-
Journal of cell science [J Cell Sci] 2023 Mar 15; Vol. 136 (6). Date of Electronic Publication: 2023 Mar 24. - Publication Year :
- 2023
-
Abstract
- Dynamin-related proteins (Drps) mediate a variety of membrane remodelling processes. The Saccharomyces cerevisiae Drp, Vps1, is required for endocytosis, endosomal sorting, vacuole fusion, and peroxisome fission and breakdown. How Drps, and in particular Vps1, can function at so many different subcellular locations is of interest to our understanding of cellular organisation. We found that the peroxisomal membrane protein Pex27 is specifically required for Vps1-dependent peroxisome fission in proliferating cells but is not required for Dnm1-dependent peroxisome fission. Pex27 accumulates in constricted regions of peroxisomes and affects peroxisome geometry upon overexpression. Moreover, Pex27 physically interacts with Vps1 in vivo and is required for the accumulation of a GTPase-defective Vps1 mutant (K42A) on peroxisomes. During nitrogen starvation, a condition that halts cell division and induces peroxisome breakdown, Vps1 associates with the pexophagophore. Pex27 is neither required for Vps1 recruitment to the pexophagophore nor for pexophagy. Our study identifies Pex27 as a Vps1-specific partner for the maintenance of peroxisome number in proliferating yeast cells.<br />Competing Interests: Competing interests The authors declare no competing or financial interests.<br /> (© 2023. Published by The Company of Biologists Ltd.)
- Subjects :
- Vesicular Transport Proteins genetics
Vesicular Transport Proteins metabolism
GTP-Binding Proteins metabolism
Dynamins metabolism
Intracellular Membranes metabolism
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae metabolism
Peroxisomes metabolism
Saccharomyces cerevisiae Proteins genetics
Saccharomyces cerevisiae Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1477-9137
- Volume :
- 136
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Journal of cell science
- Publication Type :
- Academic Journal
- Accession number :
- 36825558
- Full Text :
- https://doi.org/10.1242/jcs.246348