Linked Life Data

11821067

Source:http://linkedlifedata.com/resource/pubmed/id/11821067

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2002-1-31
pubmed:abstractText
We report that the Vps10p domain receptor sorLA binds the adaptor proteins GGA1 and -2, which take part in Golgi-endosome sorting. The GGAs bind with differential requirements via three critical residues in the C-terminal segment of the sorLA cytoplasmic tail. Unlike in sortilin and the mannose 6-phosphate receptors, the GGA-binding segment in sorLA contains neither an acidic cluster nor a dileucine. Our results support the concept of sorLA as a potential sorting receptor and suggest that key residues in sorLA and sortilin conform to a new type of motif (psi-psi-X-X-phi) defining minimum requirements for GGA binding to cytoplasmic receptor domains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
511
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
155-8
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding.
pubmed:affiliation
Department of Molecular and Cellular Neurobiology, Vrije Universiteit, 1081 HV Amsterdam, The Netherlands. lija@bio.vu.nl
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't