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

doi:10.1074/jbc.M113.527192

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

Chemistry (Twin Cities)

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34 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 language	English (US)
Pages (from-to)	6862-6876
Number of pages	15
Journal	Journal of Biological Chemistry
Volume	289
Issue number	10
DOIs	https://doi.org/10.1074/jbc.M113.527192
State	Published - Mar 7 2014

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Schuld, N. J., Vervacke, J. S., Lorimer, E. L., Simon, N. C., Hauser, A. D., Barbieri, J. T., Distefano, M. D., & Williams, C. L. (2014). The chaperone protein smggds interacts with small gtpases entering the prenylation pathway by recognizing the last amino acid in the CAAX motif. Journal of Biological Chemistry, 289(10), 6862-6876. https://doi.org/10.1074/jbc.M113.527192

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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.",

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AU - Vervacke, Jeffrey S.

AU - Lorimer, Ellen L.

AU - Simon, Nathan C.

AU - Hauser, Andrew D.

AU - Barbieri, Joseph T.

AU - Distefano, Mark D.

AU - Williams, Carol L.

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

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