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

Ras interaction with the GTPase-activating protein (GAP).

M D Schaber1, V M Garsky, D Boylan

  • 1Department of Molecular Biology, Merck Sharp and Dohme Research Laboratories, West Point, Pennsylvania 19486.

Proteins
|January 1, 1989
PubMed
Summary
This summary is machine-generated.

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

Genome-wide association study identifies SESTD1 as a novel risk gene for lithium-responsive bipolar disorder.

Molecular psychiatry·2017
Same author

Functional analysis of rare variants found in schizophrenia implicates a critical role for GIT1-PAK3 signaling in neuroplasticity.

Molecular psychiatry·2016
Same author

Genome-wide association study identifies SESTD1 as a novel risk gene for lithium-responsive bipolar disorder.

Molecular psychiatry·2015
Same author

Disordered breathing during sleep and exercise in idiopathic pulmonary fibrosis.

QJM : monthly journal of the Association of Physicians·2015
Same author

Analysis of exome sequence in 604 trios for recessive genotypes in schizophrenia.

Translational psychiatry·2015
Same author

Whole exome sequencing is an efficient, sensitive and specific method for determining the genetic cause of short-rib thoracic dystrophies.

Clinical genetics·2014

Ras protein binding to GTPase-activating protein (GAP) is crucial for cellular signaling. Specific mutations in Ras affect this interaction, but the [Ser-35]Ras mutant highlights complex in vivo regulation.

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Protein-Protein Interactions

Background:

  • Ras proteins are key regulators of cellular processes, interacting with GTPase-activating protein (GAP).
  • Understanding Ras-GAP interactions is vital for deciphering mammalian cell signaling pathways.
  • Mutations in Ras can disrupt its biological activity and interactions with regulatory proteins.

Purpose of the Study:

  • To investigate the structural requirements of Ras for binding to GAP.
  • To identify specific Ras residues and regions critical for GAP interaction.
  • To explore the functional consequences of Ras mutations on GAP binding and biological activity.

Main Methods:

  • Construction and testing of various mutant Ras proteins for GAP binding.

Related Experiment Videos

  • Synthesis and evaluation of Ras-derived peptides for their ability to inhibit Ras-GAP interaction.
  • In vitro assays measuring Ras-GAP binding affinity and biological activity.

    • Main Results:

    • Point mutations in the Ras effector region (residues 32-40) impaired Ras binding to GAP.
    • The [Ser-35]Ras mutant bound GAP effectively but exhibited reduced biological activity.
    • Ras peptides encompassing residues 17-44 and 17-32 competed with Ras for GAP binding, with peptide 17-32 being particularly effective.
    • A YPT1 peptide analogous to Ras 17-32 also competed for GAP binding, despite YPT1 itself not binding GAP.

    Conclusions:

    • The effector region of Ras is critical for GAP binding.
    • Residues within the 17-32 region of Ras are important determinants for Ras-GAP interaction.
    • In vivo regulation of Ras/protein interactions may involve factors beyond direct binding affinity.