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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">STRIPAK Complexes: structure, biological function, and involvement in human diseases</title><author><name sortKey="Hwang, Juyeon" sort="Hwang, Juyeon" uniqKey="Hwang J" first="Juyeon" last="Hwang">Juyeon Hwang</name></author><author><name sortKey="Pallas, David C" sort="Pallas, David C" uniqKey="Pallas D" first="David C." last="Pallas">David C. Pallas</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">24333164</idno><idno type="pmc">3927685</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3927685</idno><idno type="RBID">PMC:3927685</idno><idno type="doi">10.1016/j.biocel.2013.11.021</idno><date when="2013">2013</date><idno type="wicri:Area/Pmc/Corpus">002784</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">002784</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">STRIPAK Complexes: structure, biological function, and involvement in human diseases</title><author><name sortKey="Hwang, Juyeon" sort="Hwang, Juyeon" uniqKey="Hwang J" first="Juyeon" last="Hwang">Juyeon Hwang</name></author><author><name sortKey="Pallas, David C" sort="Pallas, David C" uniqKey="Pallas D" first="David C." last="Pallas">David C. Pallas</name></author></analytic><series><title level="j">The international journal of biochemistry & cell biology</title><idno type="ISSN">1357-2725</idno><idno type="eISSN">1878-5875</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P2">The mammalian striatin family consists of three proteins, striatin, S/G<sub>2</sub> nuclear autoantigen, and zinedin. Striatin family members have no intrinsic catalytic activity, but rather function as scaffolding proteins. Remarkably, they organize multiple diverse, large signaling complexes that participate in a variety of cellular processes. Moreover, they appear to be regulatory/targeting subunits for the major eukaryotic serine/threonine protein phosphatase 2A. In addition, striatin family members associate with germinal center kinase III kinases as well as other novel components, earning these assemblies the name striatin-interacting phosphatase and kinase (STRIPAK) complexes. Recently, there has been a great increase in functional and mechanistic studies aimed at identifying and understanding the roles of STRIPAK–like complexes in cellular processes of multiple organisms. These studies have identified novel STRIPAK or STRIPAK-like complexes and have explored their roles in specific signaling pathways. Together, the results of these studies have sparked increased interest in striatin family complexes because they have revealed roles in signaling, cell cycle control, apoptosis, vesicular trafficking, Golgi assembly, cell polarity, cell migration, neural and vascular development, and cardiac function. Moreover, STRIPAK complexes have been connected to clinical conditions, including cardiac disease, diabetes, autism, and cerebral cavernous malformation. In this review, we discuss the expression, localization, and protein domain structure of striatin family members. Then we consider the diverse complexes these proteins and their homologs form in various organisms, emphasizing what is known regarding function and regulation. Finally, we will explore possible roles of striatin family complexes in disease, especially cerebral cavernous malformation.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
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<front><journal-meta><journal-id journal-id-type="nlm-journal-id">9508482</journal-id><journal-id journal-id-type="pubmed-jr-id">8630</journal-id><journal-id journal-id-type="nlm-ta">Int J Biochem Cell Biol</journal-id><journal-id journal-id-type="iso-abbrev">Int. J. Biochem. Cell Biol.</journal-id><journal-title-group><journal-title>The international journal of biochemistry & cell biology</journal-title></journal-title-group><issn pub-type="ppub">1357-2725</issn><issn pub-type="epub">1878-5875</issn></journal-meta><article-meta><article-id pub-id-type="pmid">24333164</article-id><article-id pub-id-type="pmc">3927685</article-id><article-id pub-id-type="doi">10.1016/j.biocel.2013.11.021</article-id><article-id pub-id-type="manuscript">NIHMS548242</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>STRIPAK Complexes: structure, biological function, and involvement in human diseases</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Hwang</surname><given-names>Juyeon</given-names></name><email>jhwang8231@gmail.com</email></contrib><contrib contrib-type="author"><name><surname>Pallas</surname><given-names>David C.</given-names></name><xref rid="FN1" ref-type="author-notes">*</xref><email>dpallas@emory.edu</email></contrib><aff id="A1">Department of Biochemistry and Winship Cancer Institute, and Biochemistry, Cell, Developmental Biology Graduate Program, Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA</aff></contrib-group><author-notes><corresp id="FN1"><label>*</label>Corresponding author at: Biochemistry Department (RRC4125), Emory University School of Medicine, 1510 Clifton Road, Atlanta, GA. 30322; <email>dpallas@emory.edu</email></corresp></author-notes><pub-date pub-type="nihms-submitted"><day>24</day><month>1</month><year>2014</year></pub-date><pub-date pub-type="epub"><day>11</day><month>12</month><year>2013</year></pub-date><pub-date pub-type="ppub"><month>2</month><year>2014</year></pub-date><pub-date pub-type="pmc-release"><day>01</day><month>2</month><year>2015</year></pub-date><volume>47</volume><fpage>118</fpage><lpage>148</lpage><pmc-comment>elocation-id from pubmed: 10.1016/j.biocel.2013.11.021</pmc-comment>
<permissions><copyright-statement>© 2013 Elsevier Ltd. All rights reserved.</copyright-statement><copyright-year>2013</copyright-year></permissions><abstract><p id="P2">The mammalian striatin family consists of three proteins, striatin, S/G<sub>2</sub> nuclear autoantigen, and zinedin. Striatin family members have no intrinsic catalytic activity, but rather function as scaffolding proteins. Remarkably, they organize multiple diverse, large signaling complexes that participate in a variety of cellular processes. Moreover, they appear to be regulatory/targeting subunits for the major eukaryotic serine/threonine protein phosphatase 2A. In addition, striatin family members associate with germinal center kinase III kinases as well as other novel components, earning these assemblies the name striatin-interacting phosphatase and kinase (STRIPAK) complexes. Recently, there has been a great increase in functional and mechanistic studies aimed at identifying and understanding the roles of STRIPAK–like complexes in cellular processes of multiple organisms. These studies have identified novel STRIPAK or STRIPAK-like complexes and have explored their roles in specific signaling pathways. Together, the results of these studies have sparked increased interest in striatin family complexes because they have revealed roles in signaling, cell cycle control, apoptosis, vesicular trafficking, Golgi assembly, cell polarity, cell migration, neural and vascular development, and cardiac function. Moreover, STRIPAK complexes have been connected to clinical conditions, including cardiac disease, diabetes, autism, and cerebral cavernous malformation. In this review, we discuss the expression, localization, and protein domain structure of striatin family members. Then we consider the diverse complexes these proteins and their homologs form in various organisms, emphasizing what is known regarding function and regulation. Finally, we will explore possible roles of striatin family complexes in disease, especially cerebral cavernous malformation.</p></abstract><kwd-group><kwd>STRIPAK</kwd><kwd>Striatin</kwd><kwd>CCM</kwd><kwd>GCKIII</kwd><kwd>Disease</kwd></kwd-group><funding-group><award-group><funding-source country="United States">National Cancer Institute : NCI</funding-source><award-id>R01 CA057327 || CA</award-id></award-group></funding-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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