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Author Notes:

To whom correspondence should be addressed: Richard A. Kahn, Dept. of Biochemistry, Emory University School of Medicine, 1510 Clifton Rd., Atlanta, GA. Phone: 404-727-3561; Email: rkahn@emory.edu.

We thank James Olzmann (Stanford University) for helpful discussions and sharing data on the proteomes of different lipid droplet preparations and assistance in purifying lipid droplets from cells and Alex Schlacht (University of Alberta) for help in the phylogenetic analyses.

Subjects:

Research Funding:

This work was supported, in whole or in part, by National Institutes of Health Grant R01-GM090158 (to R. A. K.) and Grant P30-NS055077 from NINDS (to the Viral Vector and Microscopy Cores of the Emory Neuroscience Core Facilities).

This work was also supported by American Heart Association Grant 09PRE2140029 (to M. P. E.), Natural Sciences and Engineering Research Council of Canada, and an Alberta Innovates Technology Futures Discovery grant and New Faculty award (to J. B. D.).

Keywords:

  • ARF
  • Golgi
  • GTPase
  • Lipid Droplets
  • Phylogenetics
  • Arl2
  • Arl3
  • ELMO
  • GTPase-activating Protein (GAP)

ELMO Domains, Evolutionary and Functional Characterization of a Novel GTPase-activating Protein (GAP) Domain for Arf Protein Family GTPases

Tools:

Journal Title:

Journal of Biological Chemistry

Volume:

Volume 287, Number 47

Publisher:

, Pages 39538-39553

Type of Work:

Article | Final Publisher PDF

Abstract:

Background: ELMOD family proteins function either as Rac guanine nucleotide exchange factors or Arf GTPase-activating proteins. Results: The ELMOD family spans eukaryotic diversity and contains a putative catalytic arginine, essential for Arf GAP function. Conclusion: The ELMOD family is ancient, and GAP activity lies within the ELMO domain. Significance: This study establishes a function of the ELMO domain as a GTPase activating domain.

Copyright information:

© 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

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