Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 1
pubmed:dateCreated
2005-8-8
pubmed:abstractText
kir/Gem, Rad, Rem and Rem2 comprise the RGK (Rad/Gem/kir) family of Ras-related small G-proteins. Two important functions of RGK proteins are the regulation of the VDCC (voltage-dependent Ca2+ channel) activity and cell-shape remodelling. RGK proteins interact with 14-3-3 and CaM (calmodulin), but their role on RGK protein function is poorly understood. In contrast with the other RGK family members, Rem2 has been reported to bind neither 14-3-3 nor induce membrane extensions. Furthermore, although Rem2 inhibits VDCC activity, it does not prevent cell-surface transport of Ca2+ channels as has been shown for kir/Gem. In the present study, we re-examined the functions of Rem2 and its interaction with 14-3-3 and CaM. We show that Rem2 in fact does interact with 14-3-3 and CaM and induces dendrite-like extensions in COS cells. 14-3-3, together with CaM, regulates the subcellular distribution of Rem2 between the cytoplasm and the nucleus. Rem2 also interacts with the beta-subunits of VDCCs in a GTP-dependent fashion and inhibits Ca2+ channel activity by blocking the alpha-subunit expression at the cell surface. Thus Rem2 shares many previously unrecognized features with the other RGK family members.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-10091001, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-10441394, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-10727423, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-10831614, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-10836149, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-11031246, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-11280768, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-11395774, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-11423971, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-11483511, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-11911880, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-11956230, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-12114507, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-12639920, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-14623965, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-14701738, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-14744259, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-15000522, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-15167810, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-15615719, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-15860732, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-1650913, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-7809057, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-7912851, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-8248782, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-8810259, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-9115241, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-9268335, http://linkedlifedata.com/resource/pubmed/commentcorrection/15862114-9481669
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1470-8728
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
390
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
67-75
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Roles of 14-3-3 and calmodulin binding in subcellular localization and function of the small G-protein Rem2.
pubmed:affiliation
Epithelial Cell Biology Laboratory, Institute of Molecular and Cell Biology, 61 Biopolis Drive, Singapore 138673, Singapore. beguinp@imcb.a-star.edu.sg
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't