This domain has been annotated as Rac1-binding domain [, ]. It can be found in human CYRIA/CYRIB and at the N terminus of CYFIP1/2 []. CYFIP proteins are known RAC1 effectors that stimulate actin polymerization []. CYRIA/B are also localised to early macropinosomes and act to modulate their formation by regulating Rac1 signalling []. In mice, CYRIB (also known as CYRI or FAM49B) negatively regulates RAC1-driven cytoskeletal remodelling and plays a role in restricting infection mediated by Mycobacterium tuberculosis and Listeria monocytogenes [].
This entry includes CYRI (CYFIP-related Rac interactor) from Dictyostelium and its homologues, CYRIA/CYRIB, from animals. CYRI binds activated Rac1 via a domain of unknown function (DUF1394). It plays important roles in cell migration, chemotaxis and pathogen entry into cells. It controls actin dynamics through Rac1, the Scar/WAVE Complex and the Arp2/3 Complex [, ]. In mice, CYRIB (also known as CYRI or FAM49B) negatively regulates RAC1-driven cytoskeletal remodelling and plays a role in restricting infection mediated by Mycobacterium tuberculosis and Listeria monocytogenes [].
