
Frabin and other related Cdc42‐specific guanine nucleotide exchange factors couple the actin cytoskeleton with the plasma membrane
Author(s) -
Nakanishi Hiroyuki,
Takai Yoshimi
Publication year - 2008
Publication title -
journal of cellular and molecular medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.44
H-Index - 130
eISSN - 1582-4934
pISSN - 1582-1838
DOI - 10.1111/j.1582-4934.2008.00345.x
Subject(s) - pleckstrin homology domain , lamellipodium , guanine nucleotide exchange factor , cdc42 , microbiology and biotechnology , actin cytoskeleton , cytoskeleton , mdia1 , filopodia , actin remodeling , ferm domain , actin , moesin , chemistry , biology , gtpase , ezrin , biochemistry , membrane , membrane protein , cell , phosphorylation , integral membrane protein
• Introduction • Molecular structures of frabin and other related GEFs • Tissue distribution, subcellular localization and splicing variants of frabin and other related GEFs • Cellular activities of frabin and other related GEFs • Roles of the domains of frabin in cellular activities • Mode of action of frabin in cell shape changes • Mode of activation of frabin and FRG • Involvement of FGD4 / frabin and FGD1 in human diseases • Conclusions and perspectivesAbstract Frabin, together with, at least, FGD1, FGD2, FGD3 and FGD1‐related Cdc42‐GEF (FRG), is a member of a family of Cdc42‐specific gua‐nine nucleotide exchange factors (GEFs). These proteins have multiple phosphoinositide‐binding domains, including two pleckstrin homology (PH) domains and an FYVE or FERM domain. It is likely that they couple the actin cytoskeleton with the plasma membrane. Frabin associates with a specific actin structure(s) and induces the direct activation of Cdc42 in the vicinity of this structure(s), resulting in actin reorganization. Furthermore, frabin associates with a specific membrane structure(s) and induces the indirect activation of Rac in the vicinity of this structure(s), resulting in the reorganization of the actin cytoskeleton. This reorganization of the actin cytoskeleton induces cell shape changes such as the formation of filopodia and lamellipodia.