Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2007-7-4
pubmed:abstractText
A hallmark of semaphorin receptors is their interaction with multiple GTPases. Plexins, the signal transducing component of semaphorin receptors, directly associate with several GTPases. In addition, they not only recruit guaninine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs) but also are the only known integral membrane proteins that show a catalytic activity as GAPs for small GTPases. GTPases function upstream of semaphorin receptors and regulate the activity of plexins through an interaction with the cytoplasmic domain. The association of Plexin-Al (Sema3A receptor) or Plexin-B1 (Sema4D receptor) with the GTPase Rnd1 and ligand-dependent receptor clustering are required for their activity as R-Ras GAPs. The GTPases R-Ras and Rho function downstream of plexins and are required for the repulsive effects of semaphorins. In this review, I will focus on the role of GTPases in signaling by two plexins that have been analyzed in most detail, Plexin-A1 and Plexin-B1.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0065-2598
pubmed:author
pubmed:issnType
Print
pubmed:volume
600
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12-23
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
GTPases in semaphorin signaling.
pubmed:affiliation
Abteilung Molekularbiologie, Institut für Allgemeine Zoologie und Genetik, Westfälische Wilhelms-Universität, Schlogplatz 5, 48149 Münster, Germany. apuschel@uni-muenster.de
pubmed:publicationType
Journal Article, Review