Phosphorylation provides a negative mode of regulation for the yeast Rab GTPase Sec4p
The Rab family of Ras-related GTPases are part of a complex signaling circuitry in eukaryotic cells, yet we understand little about the mechanisms that underlie Rab protein participation in such signal transduction networks, or how these networks are integrated at the physiological level. Reversible...
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| Veröffentlicht in: | PloS one 2011-09, Vol.6 (9), p.e24332-e24332 |
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| creator | Heger, Christopher D Wrann, Christiane D Collins, Ruth N |
| description | The Rab family of Ras-related GTPases are part of a complex signaling circuitry in eukaryotic cells, yet we understand little about the mechanisms that underlie Rab protein participation in such signal transduction networks, or how these networks are integrated at the physiological level. Reversible protein phosphorylation is widely used by cells as a signaling mechanism. Several phospho-Rabs have been identified, however the functional consequences of the modification appear to be diverse and need to be evaluated on an individual basis. In this study we demonstrate a role for phosphorylation as a negative regulatory event for the action of the yeast Rab GTPase Sec4p in regulating polarized growth. Our data suggest that the phosphorylation of the Rab Sec4p prevents interactions with its effector, the exocyst component Sec15p, and that the inhibition may be relieved by a PP2A phosphatase complex containing the regulatory subunit Cdc55p. |
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Reversible protein phosphorylation is widely used by cells as a signaling mechanism. Several phospho-Rabs have been identified, however the functional consequences of the modification appear to be diverse and need to be evaluated on an individual basis. In this study we demonstrate a role for phosphorylation as a negative regulatory event for the action of the yeast Rab GTPase Sec4p in regulating polarized growth. Our data suggest that the phosphorylation of the Rab Sec4p prevents interactions with its effector, the exocyst component Sec15p, and that the inhibition may be relieved by a PP2A phosphatase complex containing the regulatory subunit Cdc55p.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0024332</identifier><identifier>PMID: 21931684</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Amino acids ; Biology ; Cell cycle ; Cell Cycle Proteins - metabolism ; Cellular signal transduction ; Circuits ; Computational Biology ; Cyclin-dependent kinases ; DNA Mutational Analysis ; Endoplasmic reticulum ; Exocytosis ; G proteins ; Genes ; Genetic engineering ; Genomics ; Guanosine triphosphatases ; Influenza ; Kinases ; Medical research ; Microscopy ; Molecular Sequence Data ; Phosphatases ; Phosphorylation ; Phosphoserine - metabolism ; Physics ; Physiological aspects ; Plasmids ; Protein Binding ; Protein Phosphatase 2 - metabolism ; Protein Transport ; Proteins ; rab GTP-Binding Proteins - chemistry ; rab GTP-Binding Proteins - metabolism ; Rab protein ; Regulation ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - ultrastructure ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - metabolism ; Signal transduction ; Signaling ; Vesicular Transport Proteins - metabolism ; Veterinary medicine ; Yeast</subject><ispartof>PloS one, 2011-09, Vol.6 (9), p.e24332-e24332</ispartof><rights>COPYRIGHT 2011 Public Library of Science</rights><rights>2011 Heger et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Heger, Christopher D</au><au>Wrann, Christiane D</au><au>Collins, Ruth N</au><au>Delprato, Anna Maria</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation provides a negative mode of regulation for the yeast Rab GTPase Sec4p</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2011-09-12</date><risdate>2011</risdate><volume>6</volume><issue>9</issue><spage>e24332</spage><epage>e24332</epage><pages>e24332-e24332</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>The Rab family of Ras-related GTPases are part of a complex signaling circuitry in eukaryotic cells, yet we understand little about the mechanisms that underlie Rab protein participation in such signal transduction networks, or how these networks are integrated at the physiological level. Reversible protein phosphorylation is widely used by cells as a signaling mechanism. Several phospho-Rabs have been identified, however the functional consequences of the modification appear to be diverse and need to be evaluated on an individual basis. In this study we demonstrate a role for phosphorylation as a negative regulatory event for the action of the yeast Rab GTPase Sec4p in regulating polarized growth. Our data suggest that the phosphorylation of the Rab Sec4p prevents interactions with its effector, the exocyst component Sec15p, and that the inhibition may be relieved by a PP2A phosphatase complex containing the regulatory subunit Cdc55p.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>21931684</pmid><doi>10.1371/journal.pone.0024332</doi><tpages>e24332</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Amino acids Biology Cell cycle Cell Cycle Proteins - metabolism Cellular signal transduction Circuits Computational Biology Cyclin-dependent kinases DNA Mutational Analysis Endoplasmic reticulum Exocytosis G proteins Genes Genetic engineering Genomics Guanosine triphosphatases Influenza Kinases Medical research Microscopy Molecular Sequence Data Phosphatases Phosphorylation Phosphoserine - metabolism Physics Physiological aspects Plasmids Protein Binding Protein Phosphatase 2 - metabolism Protein Transport Proteins rab GTP-Binding Proteins - chemistry rab GTP-Binding Proteins - metabolism Rab protein Regulation Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - ultrastructure Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Signal transduction Signaling Vesicular Transport Proteins - metabolism Veterinary medicine Yeast |
| title | Phosphorylation provides a negative mode of regulation for the yeast Rab GTPase Sec4p |
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