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Related Experiment Videos

The ARF-like 2 (ARL2)-binding protein, BART. Purification, cloning, and initial characterization.

J D Sharer1, R A Kahn

  • 1Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322-3050, USA.

The Journal of Biological Chemistry
|September 17, 1999
PubMed
Summary

Researchers identified BART, a novel protein that specifically binds to ARL2.GTP, suggesting it is the first identified effector protein for ARL2, distinct from ARF proteins.

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Area of Science:

  • Molecular Biology
  • Cellular Signaling

Background:

  • ARF-like proteins (ARLs) are a distinct subgroup of RAS-related GTPases with incompletely understood functions.
  • ARL2, a specific ARL, interacts with GTP-binding proteins.

Purpose of the Study:

  • To identify and characterize novel proteins that bind to ARL2.
  • To elucidate the specific interaction between ARL2 and its binding partners.

Main Methods:

  • Development of a high-affinity binding assay utilizing human ARL2's GTP binding properties.
  • Purification of a novel ARL2-binding protein from bovine brain homogenate.
  • Determination of the human cDNA sequence for the identified protein (BART) and recombinant protein expression.

Main Results:

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  • A 19-kDa protein, designated BART (Binder of Arl Two), was purified and found to bind specifically to ARL2.GTP with high affinity.
  • BART does not interact with ARL2.GDP or other RAS-related GTPases like ARF or RHO.
  • BART is expressed in all sampled tissues, and its interaction with ARL2 does not involve membrane association, differentiating it from ARF functions.

    • Conclusions:

    • BART is the first identified effector protein specifically interacting with ARL2.GTP.
    • The specific binding and lack of GTPase-activating protein activity suggest a unique role for BART in ARL2-mediated signaling pathways.