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Pkh1/2-dependent phosphorylation of Vps27 regulates ESCRT-I recruitment to endosomes
Multivesicular endosomes (MVBs) are major sorting platforms for membrane proteins and participate in plasma membrane protein turnover, vacuolar/lysosomal hydrolase delivery, and surface receptor signal attenuation. MVBs undergo unconventional inward budding, which results in the formation of intralu...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3469520/ https://www.ncbi.nlm.nih.gov/pubmed/22918958 http://dx.doi.org/10.1091/mbc.E12-01-0001 |
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author | Morvan, Joëlle Rinaldi, Bruno Friant, Sylvie |
author_facet | Morvan, Joëlle Rinaldi, Bruno Friant, Sylvie |
author_sort | Morvan, Joëlle |
collection | PubMed |
description | Multivesicular endosomes (MVBs) are major sorting platforms for membrane proteins and participate in plasma membrane protein turnover, vacuolar/lysosomal hydrolase delivery, and surface receptor signal attenuation. MVBs undergo unconventional inward budding, which results in the formation of intraluminal vesicles (ILVs). MVB cargo sorting and ILV formation are achieved by the concerted function of endosomal sorting complex required for transport (ESCRT)-0 to ESCRT-III. The ESCRT-0 subunit Vps27 is a key player in this pathway since it recruits the other complexes to endosomes. Here we show that the Pkh1/Phk2 kinases, two yeast orthologues of the 3-phosphoinositide–dependent kinase, phosphorylate directly Vps27 in vivo and in vitro. We identify the phosphorylation site as the serine 613 and demonstrate that this phosphorylation is required for proper Vps27 function. Indeed, in pkh-ts temperature-sensitive mutant cells and in cells expressing vps27(S613A), MVB sorting of the carboxypeptidase Cps1 and of the α-factor receptor Ste2 is affected and the Vps28–green fluorescent protein ESCRT-I subunit is mainly cytoplasmic. We propose that Vps27 phosphorylation by Pkh1/2 kinases regulates the coordinated cascade of ESCRT complex recruitment at the endosomal membrane. |
format | Online Article Text |
id | pubmed-3469520 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-34695202012-12-30 Pkh1/2-dependent phosphorylation of Vps27 regulates ESCRT-I recruitment to endosomes Morvan, Joëlle Rinaldi, Bruno Friant, Sylvie Mol Biol Cell Articles Multivesicular endosomes (MVBs) are major sorting platforms for membrane proteins and participate in plasma membrane protein turnover, vacuolar/lysosomal hydrolase delivery, and surface receptor signal attenuation. MVBs undergo unconventional inward budding, which results in the formation of intraluminal vesicles (ILVs). MVB cargo sorting and ILV formation are achieved by the concerted function of endosomal sorting complex required for transport (ESCRT)-0 to ESCRT-III. The ESCRT-0 subunit Vps27 is a key player in this pathway since it recruits the other complexes to endosomes. Here we show that the Pkh1/Phk2 kinases, two yeast orthologues of the 3-phosphoinositide–dependent kinase, phosphorylate directly Vps27 in vivo and in vitro. We identify the phosphorylation site as the serine 613 and demonstrate that this phosphorylation is required for proper Vps27 function. Indeed, in pkh-ts temperature-sensitive mutant cells and in cells expressing vps27(S613A), MVB sorting of the carboxypeptidase Cps1 and of the α-factor receptor Ste2 is affected and the Vps28–green fluorescent protein ESCRT-I subunit is mainly cytoplasmic. We propose that Vps27 phosphorylation by Pkh1/2 kinases regulates the coordinated cascade of ESCRT complex recruitment at the endosomal membrane. The American Society for Cell Biology 2012-10-15 /pmc/articles/PMC3469520/ /pubmed/22918958 http://dx.doi.org/10.1091/mbc.E12-01-0001 Text en © 2012 Morvan et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell BD; are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Morvan, Joëlle Rinaldi, Bruno Friant, Sylvie Pkh1/2-dependent phosphorylation of Vps27 regulates ESCRT-I recruitment to endosomes |
title | Pkh1/2-dependent phosphorylation of Vps27 regulates ESCRT-I recruitment to endosomes |
title_full | Pkh1/2-dependent phosphorylation of Vps27 regulates ESCRT-I recruitment to endosomes |
title_fullStr | Pkh1/2-dependent phosphorylation of Vps27 regulates ESCRT-I recruitment to endosomes |
title_full_unstemmed | Pkh1/2-dependent phosphorylation of Vps27 regulates ESCRT-I recruitment to endosomes |
title_short | Pkh1/2-dependent phosphorylation of Vps27 regulates ESCRT-I recruitment to endosomes |
title_sort | pkh1/2-dependent phosphorylation of vps27 regulates escrt-i recruitment to endosomes |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3469520/ https://www.ncbi.nlm.nih.gov/pubmed/22918958 http://dx.doi.org/10.1091/mbc.E12-01-0001 |
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