The RGS proteins add to the diversity of soybean heterotrimeric G-protein signaling
Identifieur interne : 000A07 ( Pmc/Curation ); précédent : 000A06; suivant : 000A08The RGS proteins add to the diversity of soybean heterotrimeric G-protein signaling
Auteurs : Swarup Roy Choudhury [États-Unis] ; Corey S. Westfall [États-Unis] ; Sona Pandey [États-Unis]Source :
- Plant Signaling & Behavior [ 1559-2316 ] ; 2012.
Abstract
Regulator of G-protein signaling (RGS) proteins are a family of highly diverse, multifunctional proteins that function primarily as GTPase accelerating proteins (GAPs). RGS proteins increase the rate of GTP hydrolysis by Gα proteins and essentially regulate the duration of active signaling. Recently, we have identified two chimeric RGS proteins from soybean and reported their distinct GAP activities on individual Gα proteins. A single amino acid substitution (Alanine 357 to Valine) of RGS2 is responsible for differential GAP activity. Surprisingly, most monocot plant genomes do not encode for a RGS protein homolog. Here we discuss the soybean RGS proteins in the context of their evolution in plants, their relatedness to non-plant RGS protein homologs and the effect they might have on the heterotrimeric G-protein signaling mechanisms. We also provide experimental evidence to show that the interaction interface between plant RGS and Gα proteins is different from what is predicted based on mammalian models.
Url:
DOI: 10.4161/psb.21298
PubMed: 22899066
PubMed Central: 3489640
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Westfall</name><affiliation wicri:level="2"><nlm:aff id="A2">Department of Biology; Washington University; St. Louis, MO USA</nlm:aff><country>États-Unis</country><placeName><region type="state">Missouri (État)</region></placeName><wicri:cityArea>Department of Biology; Washington University; St. Louis</wicri:cityArea></affiliation></author><author><name sortKey="Pandey, Sona" sort="Pandey, Sona" uniqKey="Pandey S" first="Sona" last="Pandey">Sona Pandey</name><affiliation wicri:level="2"><nlm:aff id="A1">Donald Danforth Plant Science Center; St. Louis, MO USA</nlm:aff><country>États-Unis</country><placeName><region type="state">Missouri (État)</region></placeName><wicri:cityArea>Donald Danforth Plant Science Center; St. Louis</wicri:cityArea></affiliation></author></analytic><series><title level="j">Plant Signaling & Behavior</title><idno type="ISSN">1559-2316</idno><idno type="eISSN">1559-2324</idno><imprint><date when="2012">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Regulator of G-protein signaling (RGS) proteins are a family of highly diverse, multifunctional proteins that function primarily as GTPase accelerating proteins (GAPs). RGS proteins increase the rate of GTP hydrolysis by Gα proteins and essentially regulate the duration of active signaling. Recently, we have identified two chimeric RGS proteins from soybean and reported their distinct GAP activities on individual Gα proteins. A single amino acid substitution (Alanine 357 to Valine) of RGS2 is responsible for differential GAP activity. Surprisingly, most monocot plant genomes do not encode for a RGS protein homolog. Here we discuss the soybean RGS proteins in the context of their evolution in plants, their relatedness to non-plant RGS protein homologs and the effect they might have on the heterotrimeric G-protein signaling mechanisms. We also provide experimental evidence to show that the interaction interface between plant RGS and Gα proteins is different from what is predicted based on mammalian models.</p></div></front></TEI><pmc article-type="brief-report"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Plant Signal Behav</journal-id><journal-id journal-id-type="iso-abbrev">Plant Signal Behav</journal-id><journal-id journal-id-type="publisher-id">PSB</journal-id><journal-title-group><journal-title>Plant Signaling & Behavior</journal-title></journal-title-group><issn pub-type="ppub">1559-2316</issn><issn pub-type="epub">1559-2324</issn><publisher><publisher-name>Landes Bioscience</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">22899066</article-id><article-id pub-id-type="pmc">3489640</article-id><article-id pub-id-type="publisher-id">2012PSB0208R</article-id><article-id pub-id-type="doi">10.4161/psb.21298</article-id><article-id pub-id-type="pii">21298</article-id><article-categories><subj-group subj-group-type="heading"><subject>Short Communication</subject></subj-group></article-categories><title-group><article-title>The RGS proteins add to the diversity of soybean heterotrimeric G-protein signaling</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Choudhury</surname><given-names>Swarup Roy</given-names></name><xref ref-type="aff" rid="A1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Westfall</surname><given-names>Corey S.</given-names></name><xref ref-type="aff" rid="A2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Pandey</surname><given-names>Sona</given-names></name><xref ref-type="aff" rid="A1"><sup>1</sup></xref><xref ref-type="corresp" rid="cor1">*</xref></contrib><aff id="A1"><label>1</label>Donald Danforth Plant Science Center; St. Louis, MO USA</aff><aff id="A2"><label>2</label>Department of Biology; Washington University; St. Louis, MO USA</aff></contrib-group><author-notes><corresp id="cor1"><label>*</label>Correspondence to: Sona Pandey, Email: <email xlink:href="spandey@danforthcenter.org">spandey@danforthcenter.org</email></corresp></author-notes><pub-date pub-type="ppub"><day>01</day><month>9</month><year>2012</year></pub-date><volume>7</volume><issue>9</issue><fpage>1114</fpage><lpage>1117</lpage><permissions><copyright-statement>Copyright © 2012 Landes Bioscience</copyright-statement><copyright-year>2012</copyright-year></permissions><abstract><p>Regulator of G-protein signaling (RGS) proteins are a family of highly diverse, multifunctional proteins that function primarily as GTPase accelerating proteins (GAPs). RGS proteins increase the rate of GTP hydrolysis by Gα proteins and essentially regulate the duration of active signaling. Recently, we have identified two chimeric RGS proteins from soybean and reported their distinct GAP activities on individual Gα proteins. A single amino acid substitution (Alanine 357 to Valine) of RGS2 is responsible for differential GAP activity. Surprisingly, most monocot plant genomes do not encode for a RGS protein homolog. Here we discuss the soybean RGS proteins in the context of their evolution in plants, their relatedness to non-plant RGS protein homologs and the effect they might have on the heterotrimeric G-protein signaling mechanisms. We also provide experimental evidence to show that the interaction interface between plant RGS and Gα proteins is different from what is predicted based on mammalian models.</p></abstract><kwd-group kwd-group-type="author"><title>Keywords: </title><kwd>RGS proteins</kwd><kwd>heterotrimeric G-proteins</kwd><kwd>soybean</kwd><kwd>protein-protein interaction</kwd><kwd>G-protein evolution</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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