Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D
We have shown previously that the betagamma subunits of the heterotrimeric G proteins regulate the organization of the pericentriolarly localized Golgi stacks. In this report, evidence is presented that the downstream target of Gbetagamma is protein kinase D (PKD), an isoform of protein kinase C. PK...
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| Veröffentlicht in: | Cell 1999-07, Vol.98 (1), p.59-68 |
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| creator | Jamora, C Yamanouye, N Van Lint, J Laudenslager, J Vandenheede, J R Faulkner, D J Malhotra, V |
| description | We have shown previously that the betagamma subunits of the heterotrimeric G proteins regulate the organization of the pericentriolarly localized Golgi stacks. In this report, evidence is presented that the downstream target of Gbetagamma is protein kinase D (PKD), an isoform of protein kinase C. PKD, unlike other members of this class of serine/threonine kinases, contains a pleckstrin homology (PH) domain. Our results demonstrate that Gbetagamma directly activates PKD by interacting with its PH domain. Inhibition of PKD activity through the use of pharmacological agents, synthetic peptide substrates, and, more specifically, the PH domain of PKD prevents Gbetagamma-mediated Golgi breakdown. Our findings suggest a possible mechanism by which the direct interaction of Gbetagamma with PKD regulates the dynamics of Golgi membranes and protein secretion. |
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In this report, evidence is presented that the downstream target of Gbetagamma is protein kinase D (PKD), an isoform of protein kinase C. PKD, unlike other members of this class of serine/threonine kinases, contains a pleckstrin homology (PH) domain. Our results demonstrate that Gbetagamma directly activates PKD by interacting with its PH domain. Inhibition of PKD activity through the use of pharmacological agents, synthetic peptide substrates, and, more specifically, the PH domain of PKD prevents Gbetagamma-mediated Golgi breakdown. Our findings suggest a possible mechanism by which the direct interaction of Gbetagamma with PKD regulates the dynamics of Golgi membranes and protein secretion.</description><identifier>ISSN: 0092-8674</identifier><identifier>PMID: 10412981</identifier><language>eng</language><publisher>United States</publisher><subject>Animals ; Binding Sites ; Biological Transport ; Cell Line ; DNA, Complementary ; Enzyme Activation ; Enzyme Inhibitors - pharmacology ; Golgi Apparatus - physiology ; Golgi Apparatus - ultrastructure ; GTP-Binding Protein beta Subunits ; GTP-Binding Protein gamma Subunits ; GTP-Binding Proteins - metabolism ; Heterotrimeric GTP-Binding Proteins ; Humans ; Kinetics ; Membrane Glycoproteins ; Mice ; Protein Kinase C - chemistry ; Protein Kinase C - metabolism ; Rats ; src Homology Domains ; Vesicular stomatitis Indiana virus ; Viral Envelope Proteins - pharmacokinetics</subject><ispartof>Cell, 1999-07, Vol.98 (1), p.59-68</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10412981$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jamora, C</creatorcontrib><creatorcontrib>Yamanouye, N</creatorcontrib><creatorcontrib>Van Lint, J</creatorcontrib><creatorcontrib>Laudenslager, J</creatorcontrib><creatorcontrib>Vandenheede, J R</creatorcontrib><creatorcontrib>Faulkner, D J</creatorcontrib><creatorcontrib>Malhotra, V</creatorcontrib><title>Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D</title><title>Cell</title><addtitle>Cell</addtitle><description>We have shown previously that the betagamma subunits of the heterotrimeric G proteins regulate the organization of the pericentriolarly localized Golgi stacks. In this report, evidence is presented that the downstream target of Gbetagamma is protein kinase D (PKD), an isoform of protein kinase C. PKD, unlike other members of this class of serine/threonine kinases, contains a pleckstrin homology (PH) domain. Our results demonstrate that Gbetagamma directly activates PKD by interacting with its PH domain. Inhibition of PKD activity through the use of pharmacological agents, synthetic peptide substrates, and, more specifically, the PH domain of PKD prevents Gbetagamma-mediated Golgi breakdown. Our findings suggest a possible mechanism by which the direct interaction of Gbetagamma with PKD regulates the dynamics of Golgi membranes and protein secretion.</description><subject>Animals</subject><subject>Binding Sites</subject><subject>Biological Transport</subject><subject>Cell Line</subject><subject>DNA, Complementary</subject><subject>Enzyme Activation</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Golgi Apparatus - physiology</subject><subject>Golgi Apparatus - ultrastructure</subject><subject>GTP-Binding Protein beta Subunits</subject><subject>GTP-Binding Protein gamma Subunits</subject><subject>GTP-Binding Proteins - metabolism</subject><subject>Heterotrimeric GTP-Binding Proteins</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Membrane Glycoproteins</subject><subject>Mice</subject><subject>Protein Kinase C - chemistry</subject><subject>Protein Kinase C - metabolism</subject><subject>Rats</subject><subject>src Homology Domains</subject><subject>Vesicular stomatitis Indiana virus</subject><subject>Viral Envelope Proteins - pharmacokinetics</subject><issn>0092-8674</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kMFOwzAQRH0A0VL4BeQTt0h2Gsf2ERUISJW49B5tknVqSOJgO0jw9Vhq4TTSamZ2316QNWM6z1QpixW5DuGdMaaEEFdkxVnBc634mtiqwQg9jCNkI3YWInbUY78MEK2bqDO0ckNvqfM9TPbnNLWBxqN3S39MirSzHttIoY326z82exfRTvTDThCQPt6QSwNDwNuzbsjh-emwe8n2b9Xr7mGfzaLgWSOZZEKqghfI0egyHdyZppCAum0F5qXITa67EhlwMIox2SBXiQVUyZXabsj9qTbt_1wwxHq0ocVhgAndEupSKy2Fksl4dzYuTSKvZ29H8N_132-2vwFLYCw</recordid><startdate>19990709</startdate><enddate>19990709</enddate><creator>Jamora, C</creator><creator>Yamanouye, N</creator><creator>Van Lint, J</creator><creator>Laudenslager, J</creator><creator>Vandenheede, J R</creator><creator>Faulkner, D J</creator><creator>Malhotra, V</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19990709</creationdate><title>Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D</title><author>Jamora, C ; Yamanouye, N ; Van Lint, J ; Laudenslager, J ; Vandenheede, J R ; Faulkner, D J ; Malhotra, V</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p541-b7070578414e1ef96555dfb47ae9cc5e2652f29d6e0a1af8007be18981a861883</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Animals</topic><topic>Binding Sites</topic><topic>Biological Transport</topic><topic>Cell Line</topic><topic>DNA, Complementary</topic><topic>Enzyme Activation</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Golgi Apparatus - physiology</topic><topic>Golgi Apparatus - ultrastructure</topic><topic>GTP-Binding Protein beta Subunits</topic><topic>GTP-Binding Protein gamma Subunits</topic><topic>GTP-Binding Proteins - metabolism</topic><topic>Heterotrimeric GTP-Binding Proteins</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Membrane Glycoproteins</topic><topic>Mice</topic><topic>Protein Kinase C - chemistry</topic><topic>Protein Kinase C - metabolism</topic><topic>Rats</topic><topic>src Homology Domains</topic><topic>Vesicular stomatitis Indiana virus</topic><topic>Viral Envelope Proteins - pharmacokinetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jamora, C</creatorcontrib><creatorcontrib>Yamanouye, N</creatorcontrib><creatorcontrib>Van Lint, J</creatorcontrib><creatorcontrib>Laudenslager, J</creatorcontrib><creatorcontrib>Vandenheede, J R</creatorcontrib><creatorcontrib>Faulkner, D J</creatorcontrib><creatorcontrib>Malhotra, V</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jamora, C</au><au>Yamanouye, N</au><au>Van Lint, J</au><au>Laudenslager, J</au><au>Vandenheede, J R</au><au>Faulkner, D J</au><au>Malhotra, V</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1999-07-09</date><risdate>1999</risdate><volume>98</volume><issue>1</issue><spage>59</spage><epage>68</epage><pages>59-68</pages><issn>0092-8674</issn><abstract>We have shown previously that the betagamma subunits of the heterotrimeric G proteins regulate the organization of the pericentriolarly localized Golgi stacks. In this report, evidence is presented that the downstream target of Gbetagamma is protein kinase D (PKD), an isoform of protein kinase C. PKD, unlike other members of this class of serine/threonine kinases, contains a pleckstrin homology (PH) domain. Our results demonstrate that Gbetagamma directly activates PKD by interacting with its PH domain. Inhibition of PKD activity through the use of pharmacological agents, synthetic peptide substrates, and, more specifically, the PH domain of PKD prevents Gbetagamma-mediated Golgi breakdown. Our findings suggest a possible mechanism by which the direct interaction of Gbetagamma with PKD regulates the dynamics of Golgi membranes and protein secretion.</abstract><cop>United States</cop><pmid>10412981</pmid><tpages>10</tpages></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Animals Binding Sites Biological Transport Cell Line DNA, Complementary Enzyme Activation Enzyme Inhibitors - pharmacology Golgi Apparatus - physiology Golgi Apparatus - ultrastructure GTP-Binding Protein beta Subunits GTP-Binding Protein gamma Subunits GTP-Binding Proteins - metabolism Heterotrimeric GTP-Binding Proteins Humans Kinetics Membrane Glycoproteins Mice Protein Kinase C - chemistry Protein Kinase C - metabolism Rats src Homology Domains Vesicular stomatitis Indiana virus Viral Envelope Proteins - pharmacokinetics |
| title | Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D |
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