Document Detail


Yeast Derlin Dfm1 interacts with Cdc48 and functions in ER homeostasis.
MedLine Citation:
PMID:  17083136     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Recent studies have identified Derlin-1, a protein that associates with the AAA-ATPase p97 and is implicated in late steps in ER-associated protein degradation (ERAD). Derlin-1 has two Saccharomyces cerevisiae homologues, Der1p and Dfm1p. While Der1p has been studied extensively, little is known about Dfm1p. Accordingly, we investigated the role of Dfm1p in ERAD, ER homeostasis and interactions with the yeast p97 homologue Cdc48p. Dfm1p was not involved in the degradation of a number of Der1-dependent or -independent ERAD substrates, neither was it redundant with either Der1p or Sec61p in ERAD. However, Dfm1p had a role in ER homeostasis, since Dfm1p loss or overexpression could stimulate the unfolded protein response (UPR). Furthermore, Dfm1p interacted both genetically and physically with Cdc48p, the yeast p97 homologue, and this interaction required an eight amino acid sequence found in the C-terminus of Dfm1p that we have termed the SHP box. Our genetic studies are consistent with the lack of a role for Dfm1p in ERAD, but indicate it participates in ER-related Cdc48p actions distinct from retrotranslocation. Finally, sequence analysis indicated that the UPR-related and Cdc48p interaction functions of Dfm1p could be separated, implying this protein probably has numerous actions in the cell. Thus, the interaction between Derlins and p97 is conserved between yeast and mammals, although its function in ERAD is not. Furthermore, Dfm1p interacts with Cdc48p through its SHP boxes, and so defines a new motif for interaction with this widely-employed AAA-ATPase.
Authors:
Brian K Sato; Randolph Y Hampton
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural    
Journal Detail:
Title:  Yeast (Chichester, England)     Volume:  23     ISSN:  0749-503X     ISO Abbreviation:  Yeast     Publication Date:    2006 Oct-Nov
Date Detail:
Created Date:  2006-11-09     Completed Date:  2007-01-12     Revised Date:  2009-09-03    
Medline Journal Info:
Nlm Unique ID:  8607637     Medline TA:  Yeast     Country:  England    
Other Details:
Languages:  eng     Pagination:  1053-64     Citation Subset:  IM    
Copyright Information:
Copyright (c) 2006 John Wiley & Sons, Ltd.
Affiliation:
UCSD Division of Biological Sciences, Section of Cell and Developmental Biology, La Jolla, CA 92093, USA.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases
Alleles
Cell Cycle Proteins / genetics,  metabolism*
Endoplasmic Reticulum / metabolism*,  physiology*
Homeostasis
Humans
Membrane Proteins / genetics,  metabolism*
Phylogeny
Protein Folding
Saccharomyces cerevisiae / physiology*
Saccharomyces cerevisiae Proteins / genetics*,  metabolism
Grant Support
ID/Acronym/Agency:
GM07240/GM/NIGMS NIH HHS; GM51996-06/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Cell Cycle Proteins; 0/DER1 protein, S cerevisiae; 0/Membrane Proteins; 0/Saccharomyces cerevisiae Proteins; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/CDC48 protein

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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