Frabin and other related Cdc42-specific guanine nucleotide exchange factors couple the actin cytoskeleton with the plasma membrane |
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Authors: | Nakanishi Hiroyuki Takai Yoshimi |
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Affiliation: | Department of Molecular Pharmacology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto, Japan. |
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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. |
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Keywords: | frabin FGD1 guanine nucleotide exchange factor Cdc42 Rac actin cytoskeleton plasma membrane filopodia lamellipodia |
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