Ontology highlight
ABSTRACT:
SUBMITTER: Nakamura K
PROVIDER: S-EPMC3408144 | biostudies-literature | 2012 Jul
REPOSITORIES: biostudies-literature
Nakamura Kensuke K Man Zhiqiu Z Xie Yong Y Hanai Ayako A Makyio Hisayoshi H Kawasaki Masato M Kato Ryuichi R Shin Hye-Won HW Nakayama Kazuhisa K Wakatsuki Soichi S
The Journal of biological chemistry 20120607 30
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 ...[more]