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.pdfVIP

Membranes 2012, 2, 91-117; doi:10.3390/membranes2010091 OPEN ACCESS 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