Linked Life Data

1939135

Source:http://linkedlifedata.com/resource/pubmed/id/1939135

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
31
pubmed:dateCreated
1991-12-13
pubmed:abstractText
The CDC42Hs protein appears to be an isoform of the ras-related GTP-binding protein G25K and is an apparent human homolog of the Saccharomyces cerevisiae cell-division-cycle protein, CDC42Sc. In this study, we report the identification of a GTPase-activating protein (GAP) for CDC42Hs from human platelets (designated from here on as CDC42Hs-GAP). The CDC42Hs-GAP activity was solubilized from platelet membranes, recovered through successive chromatography steps (the final step being Mono-Q chromatography), and purified approximately 3500-fold. The CDC42Hs-GAP activity appeared to correspond to a polypeptide with an apparent Mr of approximately 25,000. The GTPase activities of the purified human platelet CDC42Hs, the Escherichia coli-recombinant CDC42Hs, and the Spodoptera frugiperda-recombinant GTP-binding proteins are all stimulated by the CDC42Hs-GAP to identical extents, which indicates that the recombinant CDC42Hs proteins are as effective as the native human platelet protein in coupling to the GAP. However, a mutant form of the E. coli-recombinant CDC42Hs which contains a valine residue at position 12 (CDC42HsVal-12) has a significantly reduced intrinsic GTPase activity (relative to the wild type CDC42HsGly-12) which is not stimulated by the CDC42Hs-GAP. The CDC42Hs-GAP also does not stimulate the GTPase activities of the ras or rap GTP-binding proteins; however, it is capable of a weak stimulation of the GTPase activity of mammalian rho. Based on the apparent similarities in the molecular size of the CDC42Hs- and rho-GAPs (i.e. 25-30 kDa), and the cross-reactivity of rho with the CDC42Hs-GAP, it seems likely that the CDC42Hs- and rho-GAPs will constitute a specific subclass of the ras-related GAP superfamily.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
20840-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:1939135-Blood Platelets, pubmed-meshheading:1939135-Chromatography, pubmed-meshheading:1939135-Cloning, Molecular, pubmed-meshheading:1939135-Enzyme Activation, pubmed-meshheading:1939135-GTP Phosphohydrolases, pubmed-meshheading:1939135-GTP-Binding Proteins, pubmed-meshheading:1939135-GTPase-Activating Proteins, pubmed-meshheading:1939135-Guanosine Diphosphate, pubmed-meshheading:1939135-Guanosine Triphosphate, pubmed-meshheading:1939135-Humans, pubmed-meshheading:1939135-Membrane Proteins, pubmed-meshheading:1939135-Proteins, pubmed-meshheading:1939135-Recombinant Proteins, pubmed-meshheading:1939135-Structure-Activity Relationship, pubmed-meshheading:1939135-Substrate Specificity, pubmed-meshheading:1939135-cdc42 GTP-Binding Protein, pubmed-meshheading:1939135-ras GTPase-Activating Proteins
pubmed:year
1991
pubmed:articleTitle
Identification of the human platelet GTPase activating protein for the CDC42Hs protein.
pubmed:affiliation
Department of Biochemistry, Cellular and Molecular Biology, Cornell University, Ithaca, New York 14853.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't