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Related Experiment Videos

RIC, a calmodulin-binding Ras-like GTPase

P D Wes1, M Yu, C Montell

  • 1Department of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, MD 21205, USA.

The EMBO Journal
|November 1, 1996
PubMed
Summary
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Researchers identified RIC, a novel Ras-like GTPase that binds calmodulin and lacks prenylation signals. Related human proteins RIN and RIT suggest a conserved RIC family involved in neuronal signaling.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Signaling

Background:

  • Neuronal activity elevates cytosolic Ca2+, a crucial second messenger.
  • Calmodulin is a key mediator of Ca2+ signals in the nervous system.

Purpose of the Study:

  • To identify novel calmodulin-binding proteins involved in neuronal signaling.
  • To characterize the identified protein and its family members.

Main Methods:

  • Protein screening for calmodulin-binding activity.
  • Sequence analysis and comparison of identified proteins.
  • Expression pattern analysis.

Main Results:

  • Identification of RIC, a Ras-related GTPase that binds calmodulin.

Related Experiment Videos

  • RIC lacks a prenylation signal and possesses a unique G2 effector domain.
  • Discovery of human homologs RIN and RIT, also lacking prenylation signals.
  • RIN expression is specific to the nervous system, while RIC and RIT are widely expressed.

    • Conclusions:

    • RIC represents a novel class of Ras-like GTPases.
    • The RIC family, including RIN and RIT, is conserved across species.
    • RIN's neuronal specificity suggests a role in nervous system function.