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EMBO reports 5, 3, 250–255 (2004)
doi:10.1038/sj.embor.7400105
The BAR-domain family of proteins: a case of bending and binding?
The membrane bending and GTPase-binding functions of proteins
from the BAR-domain family
Bianca Habermann
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Scionics Computer
Innovation, GmbH, c/o Max Planck Institute of Molecular Cell Biology and
Genetics, Pfotenhauerstrasse 108, 01307 Dresden,
Germany Tel: +49 351 210 2543; Fax: +49 351 210 2000;
e-mail: habermann@mpi-cbg.de
Received 8 December 2003; Accepted 27 January 2004.
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Abstract
BAR-domains recently took centre stage in science through a report on
the crystal structure of this domain in Drosophila Amphiphysin. Though
only weakly conserved at the sequence level, the structure of the BAR domain
shows striking similarity to the GTPase-binding domain of Arfaptin 2, an
effector of Rho- and Arf- GTPases. On the basis of this sequence and structural
similarity, these two proteins have been classified as belonging to the same
family, the BAR-domain family, and they probably also have similar functional
characteristics. Presented here are the results of a database search for the
sequence of the BAR domain of Amphiphysin and Arfaptin 2. This search
identified a variety of related proteins, most of which are involved in
intracellular transport and especially in endocytosis. For example, the
BAR-domain family includes Endophilins, GTPase-activating proteins of the
Centaurin family and Oligophrenins, the adaptor proteins APPL1 and APPL2
that were recently shown to interact with the small GTPase Rab5, as well as
members of the Sorting nexin family. On the basis of the structures of
Amphiphysin and Arfaptin 2 and the cellular role of Amphiphysins in the early
steps of endocytosis, the functions of the BAR domain have been defined as a
dimerization motif and as sensing and inducing membrane curvature. However,
data on Arfaptin 2 and now also on the Adaptor proteins APPL1 and 2 suggest
that another function of the BAR domain is to bind to small GTPases.
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