Dataset Information


Structural basis for membrane binding specificity of the Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-2 determined by Arl1 GTPase.

ABSTRACT: Membrane-sculpting BAR (Bin/Amphiphysin/Rvs) domains form a crescent-shaped homodimer that can sense and induce membrane curvature through its positively charged concave face. We have recently shown that Arfaptin-2, which was originally identified as a binding partner for the Arf and Rac1 GTPases, binds to Arl1 through its BAR domain and is recruited onto Golgi membranes. There, Arfaptin-2 induces membrane tubules. Here, we report the crystal structure of the Arfaptin-2 BAR homodimer in complex with two Arl1 molecules bound symmetrically to each side, leaving the concave face open for membrane association. The overall structure of the Arl1·Arfaptin-2 BAR complex closely resembles that of the PX-BAR domain of sorting nexin 9, suggesting similar mechanisms underlying BAR domain targeting to specific organellar membranes. The Arl1·Arfaptin-2 BAR structure suggests that one of the two Arl1 molecules competes with Rac1, which binds to the concave face of the Arfaptin-2 BAR homodimer and may hinder its membrane association.

SUBMITTER: Nakamura K 

PROVIDER: S-EPMC3408144 | BioStudies | 2012-01-01

REPOSITORIES: biostudies

Similar Datasets

2011-01-01 | S-EPMC3064211 | BioStudies
2015-01-01 | S-EPMC4366199 | BioStudies
2006-01-01 | S-EPMC1622778 | BioStudies
2006-01-01 | S-EPMC2572078 | BioStudies
2010-01-01 | S-EPMC2888429 | BioStudies
1000-01-01 | S-EPMC5295583 | BioStudies
2011-01-01 | S-EPMC3008210 | BioStudies
2004-01-01 | S-EPMC1299016 | BioStudies
2014-01-01 | S-EPMC4021469 | BioStudies
1000-01-01 | S-EPMC3128535 | BioStudies