Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

RAP2B: a RAS-related GTP-binding protein from platelets.

C A Ohmstede1, F X Farrell, B R Reep

  • 1Division of Cell Biology, Burroughs Wellcome Co., Research Triangle Park, NC 27709.

Proceedings of the National Academy of Sciences of the United States of America
|September 1, 1990
PubMed
Summary

Researchers identified RAP2B, a novel GTP-binding protein in human platelets, closely related to RAP2. This protein, distinct from RAP1A and RAP1B, does not undergo phosphorylation by cAMP-dependent protein kinase.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Distinct effects of Re- and S-forms of LPS on modulating platelet activation.

Journal of thrombosis and haemostasis : JTH·2013
Same author

Potential therapeutic targeting of platelet-mediated cellular interactions in atherosclerosis and inflammation.

Current medicinal chemistry·2011
Same author

The role of platelets in defence against pathogens.

Hamostaseologie·2011
Same author

Classification and nomenclature of snake venom C-type lectins and related proteins.

Toxicon : official journal of the International Society on Toxinology·2009
Same author

Scientific and standardization committee communications: classification and nomenclature of snake venom C-type lectins and related proteins.

Journal of thrombosis and haemostasis : JTH·2008
Same author

Snake venom C-type lectins as tools in platelet research.

Platelets·2006

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • RAS-encoded p21 proteins play crucial roles in cellular signaling pathways.
  • RAP proteins are a family of low molecular weight GTP-binding proteins homologous to RAS.
  • Understanding novel GTP-binding proteins in platelets is essential for platelet function research.

Purpose of the Study:

  • To identify and characterize novel GTP-binding proteins in human platelets.
  • To determine the relationship of the newly identified protein to the RAP family.
  • To investigate the functional properties of the novel protein, including GTP binding and phosphorylation.

Main Methods:

  • Screening of a human platelet cDNA expression library using a monoclonal antibody against RAS-encoded p21 proteins.

Related Experiment Videos

  • DNA sequencing to identify the encoded protein and its relationship to known proteins.
  • Isolation of full-length cDNA and expression in Escherichia coli.
  • Biochemical analysis including GTP binding assays and protein phosphorylation studies.

    • Main Results:

    • Identification and cloning of a novel protein, RAP2B, closely related to RAP2.
    • RAP2B shares 90% amino acid identity with RAP2, with variations at the carboxyl terminus.
    • Expressed RAP2B is a 22,000 Mr GTP-binding protein.
    • RAP2B is not phosphorylated by the catalytic subunit of cAMP-dependent protein kinase, unlike RAP1A and RAP1B.

    Conclusions:

    • RAP2B is a novel low molecular weight GTP-binding protein found in human platelets.
    • RAP2B represents a distinct member of the RAP protein family with unique regulatory properties.
    • The findings contribute to the understanding of GTP-binding protein diversity and function in platelets.