The chaperone protein smggds interacts with small gtpases entering the prenylation pathway by recognizing the last amino acid in the CAAX motif

Nathan J. Schuld, Jeffrey S. Vervacke, Ellen L. Lorimer, Nathan C. Simon, Andrew D. Hauser, Joseph T. Barbieri, Mark D. Distefano, Carol L. Williams

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

Background: SmgGDS-607 and SmgGDS-558 regulate GTPase movement through the prenylation pathway. Results: The specificity of SmgGDS for GTPases depends on the GTPase CAAX sequence and the cellular context. Conclusion: SmgGDS-607 binds to nonprenylated GTPases that end in a leucine and enter the geranylgeranylation pathway. Significance: The identification of SmgGDS-607 as a novel CAAX-binding protein will accelerate the development of more effective cancer therapeutics.

Original languageEnglish (US)
Pages (from-to)6862-6876
Number of pages15
JournalJournal of Biological Chemistry
Volume289
Issue number10
DOIs
StatePublished - Mar 7 2014

Bibliographical note

Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.

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