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Cited by 200Cellular transport and secretionLipid Membrane Structure and BehaviorCaveolin-1 and cellular processes

Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin

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Wang, Qi, Navarro, Marcos V. A. S., Peng, Gary, Molinelli, Evan, Lin Goh, Shih, Judson, Bret L., Rajashankar, Kanagalaghatta R., Sondermann, Holger·2009·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.0902974106PMC PMC2722316
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Abstract

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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  • Syndapin is a peripheral membrane protein located in the SSR and its F-bar domain may contribute to the folding and tubulation of this postsynaptic membrane network.

    “Syndapin is a peripheral membrane protein located in the SSR and its F-bar domain may contribute to the folding and tubulation of this postsynaptic membrane network (Kumar et al, 2009;Wang et al, 2009;Rao et al, 2010).”

    From Ral mediates activity‐dependent growth of postsynaptic membranes via recruitment of the exocyst (2013) · cites this paper as Wang et al, 2009

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Authors
Wang, Q., Navarro, M. V. A. S., Peng, G., Molinelli, E., Lin Goh, S., Judson, B. L., Rajashankar, K. R., & Sondermann, H.
Affiliations
  • Cornell University (US)
  • Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853;
  • Argonne National Laboratory (US)
ORCID
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2009-08-04
Volume
106
Issue
31
Pages
12700-12705
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.0902974106
PMC
PMC2722316
OpenAlex
W1981559490
Cited by
200
References
0
Citations by year
2026: 4 · 2025: 3 · 2024: 6 · 2023: 8 · 2022: 8 · 2021: 12 · 2020: 12 · 2019: 9 · 2018: 8 · 2017: 8 · 2016: 15 · 2015: 10 · 2014: 13 · 2013: 14 · 2012: 26
FWCI
9.54
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Science Foundation (0225180)
  • National Institutes of Health (RR15301, RR-01646)
  • Cornell Center for Materials Research
  • National Institute of General Medical Sciences (DMR-0225180)
  • National Institute of Biomedical Imaging and Bioengineering (P30EB009998)
  • Division of Materials Research (DMR-0225180)
  • National Center for Research Resources (RR-01646, RR 15301, P41RR001646, P41RR015301)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
Keywords
F-BAR domain, membrane tubulation, membrane constriction, membrane curvature, vesicle formation, endocytosis, BAR domain, protein oligomerization, autoinhibition, membrane trafficking, scaffold proteins
MeSH terms
Cell Membrane, Crystallization, Endocytosis, Humans, Liposomes, Protein Structure, Tertiary, Adaptor Proteins, Signal Transducing

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