Linked Life Data

17083136

Source:http://linkedlifedata.com/resource/pubmed/id/17083136

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14-15
pubmed:dateCreated
2006-11-9
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0749-503X
pubmed:author
pubmed:copyrightInfo
Copyright (c) 2006 John Wiley & Sons, Ltd.
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1053-64
pubmed:dateRevised
2009-9-3
pubmed:meshHeading
pubmed:articleTitle
Yeast Derlin Dfm1 interacts with Cdc48 and functions in ER homeostasis.
pubmed:affiliation
UCSD Division of Biological Sciences, Section of Cell and Developmental Biology, La Jolla, CA 92093, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural