Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/2509
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dc.contributor.authorSharma, Mahak-
dc.contributor.authorCaplan, S.-
dc.date.accessioned2020-12-02T09:28:34Z-
dc.date.available2020-12-02T09:28:34Z-
dc.date.issued2016-
dc.identifier.citationEncyclopedia of Cell Biology, 2, pp. 491-502en_US
dc.identifier.otherhttps://doi.org/10.1016/B978-0-12-394447-4.20050-3-
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/B9780123944474200503?via%3Dihub-
dc.identifier.urihttp://hdl.handle.net/123456789/2509-
dc.description.abstractThe BIN-Amphiphysin-Rvs (BAR) domain is an evolutionarily conserved region found in over 750 proteins. BAR domain superfamily members dimerize to form a surface capable of membrane sensing and binding. Such membrane remodeling is essential for the organization and function of intracellular organelles, thus influencing important cellular events including endocytic and membrane trafficking, cell cycle, division, and migration. In this article, we examine the different subfamilies of BAR domain proteins and discuss how they exert their influence to shape membranes. We also focus on the roles of key BAR domain proteins and their roles in mediating actin assembly and intracellular transport and signaling.en_US
dc.language.isoenen_US
dc.publisherElsevier Ltden_US
dc.subjectBAR domainen_US
dc.subjectClathrin-coated pitsen_US
dc.subjectCurvature-sensingen_US
dc.subjectNucleation promoting factorsen_US
dc.subjectPleckstrin homology domainen_US
dc.subjectCytoskeletonen_US
dc.titleBAR Domains and BAR Domain Superfamily Proteinsen_US
dc.typeArticleen_US
Appears in Collections:Research Articles

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