Abstract
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.
Highlights
Rho family small GTP-binding proteins (G proteins), including Cdc42, Rac and Rho, regulate the actin cytoskeleton-dependent cellular activities, including cell shape changes, cell migration, cell adhesion and cytokinesis [1, 2]
Of the actin cytoskeleton-dependent cellular activities in fibroblasts, such as NIH 3T3 and Swiss 3T3 cells, Cdc42 regulates the formation of filopodia, Rac regulates the formation of lamellipodia and ruffles and Rho regulates the formation of stress fibers and focal adhesions [1, 2]
We have described here our current knowledge of frabin and other related Cdc42-specific guanine nucleotide exchange factors (GEFs), including FGD1, FGD2, FGD3, FGD5, FGD6 and FGD1-related Cdc42-GEF (FRG)
Summary
a Department of Molecular Pharmacology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan b Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita, Japan c Division of Molecular and Cellular Biology, Department of Biochemistry and Molecular Biology, Kobe University Graduate GEFs • Tissue distribution, subcellular localization and splicing variants of frabin and other related GEFs • Cellular activities of frabin and other related GEFs • 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 perspectives
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