Cytoskeletal Interactions of Raplb in Platelets

  • Gilbert C. WhiteII
  • Neville Crawford
  • Thomas H. Fischer
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 344)

Abstract

Low molecular weight GTP binding proteins (G proteins) are membrane-associated proteins which reversibly bind guanine nucleotides and regulate cellular processes, such as growth and differentiation (Evans et al., 1991; Macara, 1991). Members of this superfamily of proteins show considerable sequence homology and share structural features, including an effector domain which interacts with GTPase activating proteins or GAPs and post-translational modification at the carboxy terminus by polyisoprenyl groups, either farnesyl or geranyl-geranyl (Maltese, 1990; Gibbs, 1991). To date, more than 50 low molecular weight G proteins in four subfamilies have been reported. The prototype for this group of proteins is p21ras the 21 kDa protein product of the ras protooncogene. At least seven distinct G proteins are present in platelets (Bhullar & Haslam, 1988; Ohmori et al., 1988; Polakis et al., 1989; Polakis et al., 1989; Farrell et al., 1990; Nemoto et al., 1992) (Table I).

Keywords

NADPH Oxidase Human Platelet Phorbol Myristate Acetate Intracellular Membrane United Kingdom Introduction 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Gilbert C. WhiteII
    • 1
  • Neville Crawford
    • 2
  • Thomas H. Fischer
    • 1
  1. 1.Center for Thrombosis and HemostasisUniversity of North CarolinaChapel HillUSA
  2. 2.Department of Biochemistry and Cell BiologyRoyal College of Surgeons of EnglandLondonUK

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