BAR Domains and BAR Domain Superfamily Proteins

M. Sharma; S. Caplan

doi:10.1016/B978-0-12-394447-4.20050-3

BAR Domains and BAR Domain Superfamily Proteins

M. Sharma, S. Caplan

Research output: Chapter in Book/Report/Conference proceeding › Chapter

1 Scopus citations

Abstract

The 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.

Original language	English (US)
Title of host publication	Organizational Cell Biology
Publisher	Elsevier Inc.
Pages	491-502
Number of pages	12
Volume	2
ISBN (Electronic)	9780123944474
ISBN (Print)	9780123947963
DOIs	https://doi.org/10.1016/B978-0-12-394447-4.20050-3
State	Published - 2016

Keywords

BAR domain
Clathrin-coated pits
Curvature-sensing
Cytoskeleton
Dimerization
Dynamin
Membrane curvature
Nucleation promoting factors
PHOX-domain
Pleckstrin homology domain

ASJC Scopus subject areas

General Medicine

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10.1016/B978-0-12-394447-4.20050-3

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title = "BAR Domains and BAR Domain Superfamily Proteins",

abstract = "The 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.",

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AU - Caplan, S.

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AB - The 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.

KW - BAR domain

KW - Clathrin-coated pits

KW - Curvature-sensing

KW - Cytoskeleton

KW - Dimerization

KW - Dynamin

KW - Membrane curvature

KW - Nucleation promoting factors

KW - PHOX-domain

KW - Pleckstrin homology domain

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M3 - Chapter

AN - SCOPUS:85042779138

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VL - 2

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BT - Organizational Cell Biology

PB - Elsevier Inc.

ER -

BAR Domains and BAR Domain Superfamily Proteins

Abstract

Keywords

ASJC Scopus subject areas

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