Document Detail

Ras GTPase-activating protein physically associates with mitogenically active phospholipids.
MedLine Citation:
PMID:  1901947     Owner:  NLM     Status:  MEDLINE    
The physical interaction between GTPase-activating protein (GAP) and lipids has been characterized by two separate analyses. First, bacterially synthesized GAP molecules were found to associate with detergent-mixed micelles containing arachidonic but not with those containing arachidic acid. This association was detected by a faster elution time during molecular exclusion chromatography. Second, GAP molecules within a crude cellular lysate were specifically retained by a column on which certain lipids had been immobilized. The lipids able to retain GAP on such columns were identical to those which were shown previously to be most active in blocking GAP activity. The association between lipids and GAP was dependent upon magnesium ions. Lipids unable to inhibit GAP activity were also unable to physically associate with GAP. The tight association of GAP with these lipids was predicted by and helps to rationalize their ability to inhibit GAP activity.
M H Tsai; M Roudebush; S Dobrowolski; C L Yu; J B Gibbs; D W Stacey
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Molecular and cellular biology     Volume:  11     ISSN:  0270-7306     ISO Abbreviation:  Mol. Cell. Biol.     Publication Date:  1991 May 
Date Detail:
Created Date:  1991-05-21     Completed Date:  1991-05-21     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  8109087     Medline TA:  Mol Cell Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2785-93     Citation Subset:  IM    
Department of Molecular Biology, Cleveland Clinic Foundation, Ohio 44106.
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MeSH Terms
Brain / metabolism*
Chromatography, Affinity
Chromatography, Gel
Cytoplasm / metabolism
Edetic Acid / pharmacology
GTPase-Activating Proteins
Guanosine Triphosphate / metabolism
Molecular Weight
Phospholipids / metabolism*
Protein Binding
Proteins / isolation & purification,  metabolism*
Structure-Activity Relationship
ras GTPase-Activating Proteins
Grant Support
48662//PHS HHS
Reg. No./Substance:
0/GTPase-Activating Proteins; 0/Liposomes; 0/Micelles; 0/Phospholipids; 0/Proteins; 0/ras GTPase-Activating Proteins; 60-00-4/Edetic Acid; 86-01-1/Guanosine Triphosphate

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