Abstract:
:Plexin-B1 regulates various cellular processes interacting directly with several Rho proteins. Molecular details of these interactions are, however, not well understood. In this study, we examined in vitro and in silico the interaction of the Rho binding domain (B1RBD) of human Plexin-B1 with 11 different Rho proteins. We show that B1RBD binds in a GTP-dependent manner to Rac1, Rac2, Rac3, Rnd1, Rnd2, Rnd3, and RhoD, but not to RhoA, Cdc42, RhoG, or Rif. Interestingly, Rnd1 competitively displaces the Rac1 from B1RBD but not vice versa. Structure-function analysis revealed a negatively charged loop region, called B1L(31), which may facilitate a selective B1RBD interaction with Rho proteins.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Fansa EK,Dvorsky R,Zhang SC,Fiegen D,Ahmadian MRdoi
10.1016/j.bbrc.2013.04.012subject
Has Abstractpub_date
2013-05-17 00:00:00pages
785-90issue
4eissn
0006-291Xissn
1090-2104pii
S0006-291X(13)00638-4journal_volume
434pub_type
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