| Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin. | |
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MedLine Citation:
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PMID: 19549836 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Peripheral membrane proteins of the Bin/amphiphysin/Rvs (BAR) and Fer-CIP4 homology-BAR (F-BAR) family participate in cellular membrane trafficking and have been shown to generate membrane tubules. The degree of membrane bending appears to be encoded in the structure and immanent curvature of the particular protein domains, with BAR and F-BAR domains inducing high- and low-curvature tubules, respectively. In addition, oligomerization and the formation of ordered arrays influences tubule stabilization. Here, the F-BAR domain-containing protein Pacsin was found to possess a unique activity, creating small tubules and tubule constrictions, in addition to the wide tubules characteristic for this subfamily. Based on crystal structures of the F-BAR domain of Pacsin and mutagenesis studies, vesiculation could be linked to the presence of unique structural features distinguishing it from other F-BAR proteins. Tubulation was suppressed in the context of the full-length protein, suggesting that Pacsin is autoinhibited in solution. The regulated deformation of membranes and promotion of tubule constrictions by Pacsin suggests a more versatile function of these proteins in vesiculation and endocytosis beyond their role as scaffold proteins. |
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Authors:
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Qi Wang; Marcos V A S Navarro; Gary Peng; Evan Molinelli; Shih Lin Goh; Bret L Judson; Kanagalaghatta R Rajashankar; Holger Sondermann |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. Date: 2009-06-19 |
Journal Detail:
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Title: Proceedings of the National Academy of Sciences of the United States of America Volume: 106 ISSN: 1091-6490 ISO Abbreviation: Proc. Natl. Acad. Sci. U.S.A. Publication Date: 2009 Aug |
Date Detail:
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Created Date: 2009-08-11 Completed Date: 2009-08-26 Revised Date: 2013-02-19 |
Medline Journal Info:
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Nlm Unique ID: 7505876 Medline TA: Proc Natl Acad Sci U S A Country: United States |
Other Details:
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Languages: eng Pagination: 12700-5 Citation Subset: IM |
Affiliation:
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Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA. |
| Data Bank Information | |
Bank Name/Acc. No.:
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PDB/3HAH; 3HAI; 3HAJ |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adaptor Proteins, Signal Transducing
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chemistry,
physiology* Cell Membrane / physiology* Crystallization Endocytosis Humans Liposomes / metabolism Protein Structure, Tertiary |
| Grant Support | |
ID/Acronym/Agency:
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P30 EB009998/EB/NIBIB NIH HHS; RR-01646/RR/NCRR NIH HHS; RR-15301/RR/NCRR NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Adaptor Proteins, Signal Transducing; 0/Liposomes; 0/PACSIN1 protein, human; 0/PACSIN2 protein, human |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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