Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
2004-4-12
pubmed:abstractText
Although many proteins have been shown to participate in mitotic events, including cytokinesis, their specific roles and interactions remain unclear. A novel interaction of proteins is demonstrated in this report. Yeast two-hybrid screening using PRC1 (protein-regulating cytokinesis 1) cDNA, a human mitotic spindle-associated cyclin-dependent kinase (CDK) substrate, which is involved in cytokinesis, as bait was performed. Data show that the PRC1 bait bound to MgcRacGAP, which is a GTPase-activating protein (GAP) for the Rho family GTPases also involved in cytokinesis. In addition, the two proteins showed similar localization during the M phase. PRC1 was shown to bind to the COOH-terminal GAP-conserved domain of MgcRacGAP and to inhibit its GAP activity toward Cdc42. This binding and/or inhibition of MgcRacGAP GAP activity was found to depend on further binding of PRC1 to the basic region (125-285 amino acids) of MgcRacGAP. Furthermore, the basic region was phosphorylated with Aurora B kinase, and this phosphorylation prevented the inhibition of GAP activity by PRC1. Cells overexpressing a phosphorylation mimic mutant of MgcRacGAP exhibited an abnormality of spindle morphology in the metaphase. Cdc42 showed high activity and was localized to the mitotic spindles and centrosomes during the metaphase. We propose that PRC1 down-regulates the GAP activity of MgcRac-GAP during the metaphase and thereby contributes to the correct formation of the spindle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16394-402
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Human mitotic spindle-associated protein PRC1 inhibits MgcRacGAP activity toward Cdc42 during the metaphase.
pubmed:affiliation
Division of Molecular Life Science, School of Life Science, Tokyo University of Pharmacy and Life Science, 1432-1 Horinouchi, Hachioji, Tokyo 192-0392, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't