ParkinsonFranceV1, Ncbi, Merge, bibRecord, 000E25

Single Point Mutation in Bin/Amphiphysin/Rvs (BAR) Sequence of Endophilin Impairs Dimerization, Membrane Shaping, and Src Homology 3 Domain-mediated Partnership*

Identifieur interne : 000E25 ( Ncbi/Merge ); précédent : 000E24; suivant : 000E26

Single Point Mutation in Bin/Amphiphysin/Rvs (BAR) Sequence of Endophilin Impairs Dimerization, Membrane Shaping, and Src Homology 3 Domain-mediated Partnership*

Auteurs : Anna Gortat [France] ; Mabel Jouve San-Roman [France] ; Christian Vannier [France] ; Anne A. Schmidt [France]

Source :

The Journal of Biological Chemistry [ 0021-9258 ] ; 2011.

RBID : PMC:3281743

Abstract

Background: The BAR domain is a dimeric module controlling membrane curvature.

Results: We identify leucine 215 involved in stabilizing the dimer interface and characterize the incidence of its substitution in SH3-mediated partnership in endophilins.

Conclusion: Altered BAR conformation/rigidity impairs membrane binding, shaping, and partnership.

Significance: This mutation in other BAR domain-containing proteins may unravel unanticipated functional relationships between the BAR domain and other structural units.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3281743

DOI: 10.1074/jbc.M111.325837
PubMed: 22167186
PubMed Central: 3281743

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PMC:3281743

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Single Point Mutation in Bin/Amphiphysin/Rvs (BAR) Sequence of Endophilin Impairs Dimerization, Membrane Shaping, and Src Homology 3 Domain-mediated Partnership<xref ref-type="fn" rid="FN1">*</xref>
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<author><name sortKey="Gortat, Anna" sort="Gortat, Anna" uniqKey="Gortat A" first="Anna" last="Gortat">Anna Gortat</name>
<affiliation wicri:level="3"><nlm:aff id="aff1">From the CNRS, UMR7592, Institut Jacques Monod, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris, France</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>From the CNRS, UMR7592, Institut Jacques Monod, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris</wicri:regionArea>
<placeName><region type="region" nuts="2">Île-de-France</region>
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<author><name sortKey="San Roman, Mabel Jouve" sort="San Roman, Mabel Jouve" uniqKey="San Roman M" first="Mabel Jouve" last="San-Roman">Mabel Jouve San-Roman</name>
<affiliation wicri:level="3"><nlm:aff id="aff1">From the CNRS, UMR7592, Institut Jacques Monod, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris, France</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>From the CNRS, UMR7592, Institut Jacques Monod, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris</wicri:regionArea>
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<author><name sortKey="Vannier, Christian" sort="Vannier, Christian" uniqKey="Vannier C" first="Christian" last="Vannier">Christian Vannier</name>
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<wicri:regionArea>From the CNRS, UMR7592, Institut Jacques Monod, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris</wicri:regionArea>
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<author><name sortKey="Schmidt, Anne A" sort="Schmidt, Anne A" uniqKey="Schmidt A" first="Anne A." last="Schmidt">Anne A. Schmidt</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Single Point Mutation in Bin/Amphiphysin/Rvs (BAR) Sequence of Endophilin Impairs Dimerization, Membrane Shaping, and Src Homology 3 Domain-mediated Partnership<xref ref-type="fn" rid="FN1">*</xref>
<xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic>
</sup>
</xref>
</title>
<author><name sortKey="Gortat, Anna" sort="Gortat, Anna" uniqKey="Gortat A" first="Anna" last="Gortat">Anna Gortat</name>
<affiliation wicri:level="3"><nlm:aff id="aff1">From the CNRS, UMR7592, Institut Jacques Monod, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris, France</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>From the CNRS, UMR7592, Institut Jacques Monod, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris</wicri:regionArea>
<placeName><region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Paris</settlement>
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</author>
<author><name sortKey="San Roman, Mabel Jouve" sort="San Roman, Mabel Jouve" uniqKey="San Roman M" first="Mabel Jouve" last="San-Roman">Mabel Jouve San-Roman</name>
<affiliation wicri:level="3"><nlm:aff id="aff1">From the CNRS, UMR7592, Institut Jacques Monod, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris, France</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>From the CNRS, UMR7592, Institut Jacques Monod, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris</wicri:regionArea>
<placeName><region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Paris</settlement>
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<author><name sortKey="Vannier, Christian" sort="Vannier, Christian" uniqKey="Vannier C" first="Christian" last="Vannier">Christian Vannier</name>
<affiliation wicri:level="3"><nlm:aff id="aff1">From the CNRS, UMR7592, Institut Jacques Monod, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris, France</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>From the CNRS, UMR7592, Institut Jacques Monod, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris</wicri:regionArea>
<placeName><region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Paris</settlement>
</placeName>
</affiliation>
</author>
<author><name sortKey="Schmidt, Anne A" sort="Schmidt, Anne A" uniqKey="Schmidt A" first="Anne A." last="Schmidt">Anne A. Schmidt</name>
<affiliation wicri:level="3"><nlm:aff id="aff1">From the CNRS, UMR7592, Institut Jacques Monod, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris, France</nlm:aff>
<country xml:lang="fr">France</country>
<wicri:regionArea>From the CNRS, UMR7592, Institut Jacques Monod, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris</wicri:regionArea>
<placeName><region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Paris</settlement>
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</affiliation>
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<series><title level="j">The Journal of Biological Chemistry</title>
<idno type="ISSN">0021-9258</idno>
<idno type="eISSN">1083-351X</idno>
<imprint><date when="2011">2011</date>
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<front><div type="abstract" xml:lang="en"><p><bold>Background:</bold>
 The BAR domain is a dimeric module controlling membrane curvature.</p>
<p><bold>Results:</bold>
 We identify leucine 215 involved in stabilizing the dimer interface and characterize the incidence of its substitution in SH3-mediated partnership in endophilins.</p>
<p><bold>Conclusion:</bold>
 Altered BAR conformation/rigidity impairs membrane binding, shaping, and partnership.</p>
<p><bold>Significance:</bold>
 This mutation in other BAR domain-containing proteins may unravel unanticipated functional relationships between the BAR domain and other structural units.</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>
  <front><journal-meta><journal-id journal-id-type="nlm-ta">J Biol Chem</journal-id>
<journal-id journal-id-type="hwp">jbc</journal-id>
<journal-id journal-id-type="pmc">jbc</journal-id>
<journal-id journal-id-type="publisher-id">JBC</journal-id>
<journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title>
</journal-title-group>
<issn pub-type="ppub">0021-9258</issn>
<issn pub-type="epub">1083-351X</issn>
<publisher><publisher-name>American Society for Biochemistry and Molecular Biology</publisher-name>
<publisher-loc>9650 Rockville Pike, Bethesda, MD 20814, U.S.A.</publisher-loc>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">22167186</article-id>
<article-id pub-id-type="pmc">3281743</article-id>
<article-id pub-id-type="publisher-id">M111.325837</article-id>
<article-id pub-id-type="doi">10.1074/jbc.M111.325837</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Cell Biology</subject>
</subj-group>
</article-categories>
<title-group><article-title>Single Point Mutation in Bin/Amphiphysin/Rvs (BAR) Sequence of Endophilin Impairs Dimerization, Membrane Shaping, and Src Homology 3 Domain-mediated Partnership<xref ref-type="fn" rid="FN1">*</xref>
<xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic>
</sup>
</xref>
</article-title>
<alt-title alt-title-type="short">Functional Relationship of BAR/SH3 Domains of Endophilin</alt-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Gortat</surname>
<given-names>Anna</given-names>
</name>
<xref ref-type="aff" rid="aff1"></xref>
<xref ref-type="author-notes" rid="FN3"><sup>1</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>San-Roman</surname>
<given-names>Mabel Jouve</given-names>
</name>
<xref ref-type="aff" rid="aff1"></xref>
</contrib>
<contrib contrib-type="author"><name><surname>Vannier</surname>
<given-names>Christian</given-names>
</name>
<xref ref-type="aff" rid="aff1"></xref>
</contrib>
<contrib contrib-type="author"><name><surname>Schmidt</surname>
<given-names>Anne A.</given-names>
</name>
<xref ref-type="aff" rid="aff1"></xref>
<xref ref-type="corresp" rid="cor1"><sup>2</sup>
</xref>
</contrib>
<aff id="aff1">From the CNRS, UMR7592, Institut Jacques Monod, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris, France</aff>
</contrib-group>
<author-notes><corresp id="cor1"><label>2</label>
 To whom correspondence should be addressed: <addr-line>CNRS, UMR7592, Institut Jacques Monod, Université Paris Diderot, Sorbonne Paris Cité, Bâtiment Buffon, 15 Rue Hélène Brion, F-75205 Paris, France.</addr-line>
 Tel.: <phone>33-1-57-27-80-12</phone>
; Fax: <fax>33-1-57-27-80-26</fax>
; E-mail: <email>schmidt.anne@ijm.univ-paris-diderot.fr</email>
.</corresp>
<fn fn-type="supported-by" id="FN3"><label>1</label>
<p>Supported by fellowships from CNRS and Association pour la Recherche sur le Cancer.</p>
</fn>
</author-notes>
<pub-date pub-type="ppub"><day>3</day>
<month>2</month>
<year>2012</year>
</pub-date>
<pub-date pub-type="epub"><day>13</day>
<month>12</month>
<year>2011</year>
</pub-date>
<volume>287</volume>
<issue>6</issue>
<fpage>4232</fpage>
<lpage>4247</lpage>
<history><date date-type="received"><day>21</day>
<month>11</month>
<year>2011</year>
</date>
</history>
<permissions><copyright-statement>© 2012 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement>
<copyright-year>2012</copyright-year>
</permissions>
<self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc00612004232.pdf"></self-uri>
<abstract abstract-type="teaser"><p><bold>Background:</bold>
 The BAR domain is a dimeric module controlling membrane curvature.</p>
<p><bold>Results:</bold>
 We identify leucine 215 involved in stabilizing the dimer interface and characterize the incidence of its substitution in SH3-mediated partnership in endophilins.</p>
<p><bold>Conclusion:</bold>
 Altered BAR conformation/rigidity impairs membrane binding, shaping, and partnership.</p>
<p><bold>Significance:</bold>
 This mutation in other BAR domain-containing proteins may unravel unanticipated functional relationships between the BAR domain and other structural units.</p>
</abstract>
<abstract><p>Bin/Amphiphysin/Rvs (BAR) domain-containing proteins are essential players in the dynamics of intracellular compartments. The BAR domain is an evolutionarily conserved dimeric module characterized by a crescent-shaped structure whose intrinsic curvature, flexibility, and ability to assemble into highly ordered oligomers contribute to inducing the curvature of target membranes. Endophilins, diverging into A and B subgroups, are BAR and SH3 domain-containing proteins. They exert activities in membrane dynamic processes such as endocytosis, autophagy, mitochondrial dynamics, and permeabilization during apoptosis. Here, we report on the involvement of the third α-helix of the endophilin A BAR sequence in dimerization and identify leucine 215 as a key residue within a network of hydrophobic interactions stabilizing the entire BAR dimer interface. With the combination of N-terminal truncation retaining the high dimerization capacity of the third α-helices of endophilin A and leucine 215 substitution by aspartate (L215D), we demonstrate the essential role of BAR sequence-mediated dimerization on SH3 domain partnership. In comparison with wild type, full-length endophilin A2 heterodimers with one protomer bearing the L215D substitution exhibit very significant changes in membrane binding and shaping activities as well as a dramatic decrease of SH3 domain partnership. This suggests that subtle changes in the conformation and/or rigidity of the BAR domain impact both the control of membrane curvature and downstream binding to effectors. Finally, we show that expression, in mammalian cells, of endophilin A2 bearing the L215D substitution impairs the endocytic recycling of transferrin receptors.</p>
</abstract>
<kwd-group><kwd>Cell Biology</kwd>
<kwd>Endocytosis</kwd>
<kwd>Membrane</kwd>
<kwd>Membrane Lipids</kwd>
<kwd>Membrane Trafficking</kwd>
<kwd>Subcellular Organelles</kwd>
<kwd>Vesicles</kwd>
<kwd>BAR Domain</kwd>
<kwd>Endophilins</kwd>
<kwd>Membrane Dynamics</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
<affiliations><list><country><li>France</li>
</country>
<region><li>Île-de-France</li>
</region>
<settlement><li>Paris</li>
</settlement>
</list>
<tree><country name="France"><region name="Île-de-France"><name sortKey="Gortat, Anna" sort="Gortat, Anna" uniqKey="Gortat A" first="Anna" last="Gortat">Anna Gortat</name>
</region>
<name sortKey="San Roman, Mabel Jouve" sort="San Roman, Mabel Jouve" uniqKey="San Roman M" first="Mabel Jouve" last="San-Roman">Mabel Jouve San-Roman</name>
<name sortKey="Schmidt, Anne A" sort="Schmidt, Anne A" uniqKey="Schmidt A" first="Anne A." last="Schmidt">Anne A. Schmidt</name>
<name sortKey="Vannier, Christian" sort="Vannier, Christian" uniqKey="Vannier C" first="Christian" last="Vannier">Christian Vannier</name>
</country>
</tree>
</affiliations>
</record>

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Single Point Mutation in Bin/Amphiphysin/Rvs (BAR) Sequence of Endophilin Impairs Dimerization, Membrane Shaping, and Src Homology 3 Domain-mediated Partnership*

Single Point Mutation in Bin/Amphiphysin/Rvs (BAR) Sequence of Endophilin Impairs Dimerization, Membrane Shaping, and Src Homology 3 Domain-mediated Partnership*

Source :

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

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Pour générer des pages wiki