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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
18
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pubmed:dateCreated |
2010-5-5
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pubmed:databankReference |
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pubmed:abstractText |
Members of the Bin/amphiphysin/Rvs (BAR) domain protein superfamily are involved in membrane remodeling in various cellular pathways ranging from endocytic vesicle and T-tubule formation to cell migration and neuromorphogenesis. Membrane curvature induction and stabilization are encoded within the BAR or Fer-CIP4 homology-BAR (F-BAR) domains, alpha-helical coiled coils that dimerize into membrane-binding modules. BAR/F-BAR domain proteins often contain an SH3 domain, which recruits binding partners such as the oligomeric membrane-fissioning GTPase dynamin. How precisely BAR/F-BAR domain-mediated membrane deformation is regulated at the cellular level is unknown. Here we present the crystal structures of full-length syndapin 1 and its F-BAR domain. Our data show that syndapin 1 F-BAR-mediated membrane deformation is subject to autoinhibition by its SH3 domain. Release from the clamped conformation is driven by association of syndapin 1 SH3 with the proline-rich domain of dynamin 1, thereby unlocking its potent membrane-bending activity. We hypothesize that this mechanism might be commonly used to regulate BAR/F-BAR domain-induced membrane deformation and to potentially couple this process to dynamin-mediated fission. Our data thus suggest a structure-based model for SH3-mediated regulation of BAR/F-BAR domain function.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-10559861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-10677033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-11082044,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-12183633,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-12224553,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-12426380,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-12709533,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-14529717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-14622578,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-14645856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-15318165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-15929943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-16326391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-16648848,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-16938488,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-17956734,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-18329367,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-18400891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-18940612,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-18954304,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-19084268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-19084269,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-19244343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-19379681,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-19379701,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-19535582,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-19549836,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-19703397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-19737524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-19749743,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-19816406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-19846719,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20404169-9635431
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1091-6490
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
4
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pubmed:volume |
107
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8213-8
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pubmed:dateRevised |
2010-9-30
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pubmed:meshHeading |
pubmed-meshheading:20404169-Amino Acid Sequence,
pubmed-meshheading:20404169-Animals,
pubmed-meshheading:20404169-COS Cells,
pubmed-meshheading:20404169-Carrier Proteins,
pubmed-meshheading:20404169-Cell Membrane,
pubmed-meshheading:20404169-Cercopithecus aethiops,
pubmed-meshheading:20404169-Crystallography, X-Ray,
pubmed-meshheading:20404169-Microscopy, Electron,
pubmed-meshheading:20404169-Molecular Sequence Data,
pubmed-meshheading:20404169-Protein Structure, Tertiary,
pubmed-meshheading:20404169-src Homology Domains
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pubmed:year |
2010
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pubmed:articleTitle |
Molecular basis for SH3 domain regulation of F-BAR-mediated membrane deformation.
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pubmed:affiliation |
Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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