ParkinsonFranceV1, Ncbi, Checkpoint, 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/Checkpoint ); 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

Affiliations:

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PMC:3281743

Le document en format XML

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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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<series><title level="j">The Journal of Biological Chemistry</title>
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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>
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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)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki