the bar domain superfamily proteins from subcellular structures to human diseases禁止域总科蛋白质亚细胞结构与人类疾病.pdf
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Membranes 2012, 2, 91-117; doi:10.3390/membranes2010091
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membranes
ISSN 2077-0375
/journal/membranes
Review
The BAR Domain Superfamily Proteins from Subcellular
Structures to Human Diseases
Fatemeh Safari and Shiro Suetsugu *
Laboratory of Membrane and Cytoskeleton Dynamics, Institute of Molecular and Cellular Biosciences,
The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
* Author to whom correspondence should be addressed; E-Mail: suetsugu@iam.u-tokyo.ac.jp;
Tel.: +81-3-5841-7954; Fax: +81-3-5841-7862.
Received: 5 January 2012; in revised form: 7 February 2012 / Accepted: 15 February 2012 /
Published: 27 February 2012
Abstract: Eukaryotic cells have complicated membrane systems. The outermost plasma
membrane contains various substructures, such as invaginations and protrusions, which are
involved in endocytosis and cell migration. Moreover, the intracellular membrane
compartments, such as autophagosomes and endosomes, are essential for cellular viability.
The Bin-Amphiphysin-Rvs167 (BAR) domain superfamily proteins are important players in
membrane remodeling through their structurally determined membrane binding surfaces. A
variety of BAR domain superfamily proteins exist, and each family member appears to be
involved in the formation of certain subcellular structures or intracellular membrane
compartments. Most of the BAR domain superfamily proteins contain SH3 domains, which
bind to the membrane scission molecule, dynamin, as well as the actin regulator
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