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Yeast Irc6p is a novel type of conserved clathrin coat accessory factor related to small G proteins

Clathrin coat accessory proteins play key roles in transport mediated by clathrin-coated vesicles. Yeast Irc6p and the related mammalian p34 are putative clathrin accessory proteins that interact with clathrin adaptor complexes. We present evidence that Irc6p functions in clathrin-mediated traffic b...

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Autores principales: Gorynia, Sabine, Lorenz, Todd C., Costaguta, Giancarlo, Daboussi, Lydia, Cascio, Duilio, Payne, Gregory S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3496615/
https://www.ncbi.nlm.nih.gov/pubmed/22993212
http://dx.doi.org/10.1091/mbc.E12-07-0507
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author Gorynia, Sabine
Lorenz, Todd C.
Costaguta, Giancarlo
Daboussi, Lydia
Cascio, Duilio
Payne, Gregory S.
author_facet Gorynia, Sabine
Lorenz, Todd C.
Costaguta, Giancarlo
Daboussi, Lydia
Cascio, Duilio
Payne, Gregory S.
author_sort Gorynia, Sabine
collection PubMed
description Clathrin coat accessory proteins play key roles in transport mediated by clathrin-coated vesicles. Yeast Irc6p and the related mammalian p34 are putative clathrin accessory proteins that interact with clathrin adaptor complexes. We present evidence that Irc6p functions in clathrin-mediated traffic between the trans-Golgi network and endosomes, linking clathrin adaptor complex AP-1 and the Rab GTPase Ypt31p. The crystal structure of the Irc6p N-terminal domain revealed a G-protein fold most related to small G proteins of the Rab and Arf families. However, Irc6p lacks G-protein signature motifs and high-affinity GTP binding. Also, mutant Irc6p lacking candidate GTP-binding residues retained function. Mammalian p34 rescued growth defects in irc6∆ cells, indicating functional conservation, and modeling predicted a similar N-terminal fold in p34. Irc6p and p34 also contain functionally conserved C-terminal regions. Irc6p/p34-related proteins with the same two-part architecture are encoded in genomes of species as diverse as plants and humans. Together these results define Irc6p/p34 as a novel type of conserved clathrin accessory protein and founding members of a new G protein–like family.
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spelling pubmed-34966152013-01-30 Yeast Irc6p is a novel type of conserved clathrin coat accessory factor related to small G proteins Gorynia, Sabine Lorenz, Todd C. Costaguta, Giancarlo Daboussi, Lydia Cascio, Duilio Payne, Gregory S. Mol Biol Cell Articles Clathrin coat accessory proteins play key roles in transport mediated by clathrin-coated vesicles. Yeast Irc6p and the related mammalian p34 are putative clathrin accessory proteins that interact with clathrin adaptor complexes. We present evidence that Irc6p functions in clathrin-mediated traffic between the trans-Golgi network and endosomes, linking clathrin adaptor complex AP-1 and the Rab GTPase Ypt31p. The crystal structure of the Irc6p N-terminal domain revealed a G-protein fold most related to small G proteins of the Rab and Arf families. However, Irc6p lacks G-protein signature motifs and high-affinity GTP binding. Also, mutant Irc6p lacking candidate GTP-binding residues retained function. Mammalian p34 rescued growth defects in irc6∆ cells, indicating functional conservation, and modeling predicted a similar N-terminal fold in p34. Irc6p and p34 also contain functionally conserved C-terminal regions. Irc6p/p34-related proteins with the same two-part architecture are encoded in genomes of species as diverse as plants and humans. Together these results define Irc6p/p34 as a novel type of conserved clathrin accessory protein and founding members of a new G protein–like family. The American Society for Cell Biology 2012-11-15 /pmc/articles/PMC3496615/ /pubmed/22993212 http://dx.doi.org/10.1091/mbc.E12-07-0507 Text en © 2012 Gorynia 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
Gorynia, Sabine
Lorenz, Todd C.
Costaguta, Giancarlo
Daboussi, Lydia
Cascio, Duilio
Payne, Gregory S.
Yeast Irc6p is a novel type of conserved clathrin coat accessory factor related to small G proteins
title Yeast Irc6p is a novel type of conserved clathrin coat accessory factor related to small G proteins
title_full Yeast Irc6p is a novel type of conserved clathrin coat accessory factor related to small G proteins
title_fullStr Yeast Irc6p is a novel type of conserved clathrin coat accessory factor related to small G proteins
title_full_unstemmed Yeast Irc6p is a novel type of conserved clathrin coat accessory factor related to small G proteins
title_short Yeast Irc6p is a novel type of conserved clathrin coat accessory factor related to small G proteins
title_sort yeast irc6p is a novel type of conserved clathrin coat accessory factor related to small g proteins
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3496615/
https://www.ncbi.nlm.nih.gov/pubmed/22993212
http://dx.doi.org/10.1091/mbc.E12-07-0507
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