Linked Life Data

17462600

Source:http://linkedlifedata.com/resource/pubmed/id/17462600

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2007-5-14
pubmed:abstractText
Rab7, a member of the Rab family small G proteins, is involved in the late stage of the endocytic pathway. We previously identified a Rab7 target protein, Rabring7, which contains a RING finger domain at its C termini, but the precise role of Rabring7 remains unknown. In this study, we demonstrate using an in vitro ubiquitination assay with recombinant E1 and E2 proteins that Rabring7 has E3 ligase activity and that it preferentially reacts with Ubc4 and Ubc5 as its E2 proteins. Rabring7 ubiquitinated itself but not Rab7, and a mutation at Cys-229 in the RING finger domain (Rabring7C229S) completely diminished its E3 ligase activity. In the ligand-induced degradation of EGF receptor (EGFR), Rabring7 accelerated the degradation of EGFR, whereas Rabring7C229S inhibited the degradation induced by cCbl, another E3 ligase. These results suggest that Rabring7 is involved in the endocytic trafficking of EGFR through its E3 ligase activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
357
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1058-64
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Involvement of Rabring7 in EGF receptor degradation as an E3 ligase.
pubmed:affiliation
Department of Biochemistry, Institute of Health Biosciences, The University of Tokushima Graduate School, Tokushima 770-8503, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't