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

• Type of Material: Article
• Authors: Michael P. East, Emory University; J. Bradford Bowzard, Emory University; Joel B. Dacks, University of Alberta; Richard A Kahn, Emory University
• Language: English
• Date: 2012-11-16
• Publisher: American Society for Biochemistry and Molecular Biology
• Publication Version: Final Published Version
• Copyright Statement: © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.
• Final Published Version (URL): http://www.jbc.org/content/287/47/39538#fn-2
• Title of Journal or Parent Work: Journal of Biological Chemistry
• ISSN: 0021-9258
• Volume: 287
• Issue: 47
• Start Page: 39538
• End Page: 39553
• Grant/Funding Information: 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: GTPase-activating Protein (GAP); Phylogenetics; Arl2; Arl3; ARF; ELMO; Golgi; Lipid Droplets; GTPase
• Research Categories: Chemistry, Biochemistry; Biology, Cell

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.