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http://purl.uniprot.org/citations/20404169http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20404169http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20404169http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1003478107"xsd:string
http://purl.uniprot.org/citations/20404169http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1003478107"xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Luo L."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Luo L."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Saenger W."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Saenger W."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Ma Q."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Ma Q."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Rao Y."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Rao Y."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Haucke V."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Haucke V."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Puchkov D."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Puchkov D."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Pechstein A."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Pechstein A."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Shupliakov O."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Shupliakov O."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Vahedi-Faridi A."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Vahedi-Faridi A."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Sundborger A."xsd:string
http://purl.uniprot.org/citations/20404169http://purl.uniprot.org/core/author"Sundborger A."xsd:string