title: FERM family proteins and their importance in cellular movements and wound healing (review).
abstract: Motility is a requirement for a number of biological processes, including embryonic development, neuronal development, immune responses, cancer progression and wound healing. Specific to wound healing is the migration of endothelial cells, fibroblasts and other key cellular players into the wound space. Aberrations in wound healing can result in either chronic wounds or abnormally healed wounds. The protein 4.1R, ezrin, radixin, moesin (FERM) superfamily consists of over 40 proteins all containing a three lobed N-terminal FERM domain which binds a variety of cell-membrane associated proteins and lipids. The C-terminal ends of these proteins typically contain an actin-binding domain (ABD). These proteins therefore mediate the linkage between the cell membrane and the actin cytoskeleton, and are involved in cellular movements and migration. Certain FERM proteins have been shown to promote cancer metastasis via this very mechanism. Herein we review the effects of a number of FERM proteins on wound healing and cancer. We show how these proteins typically aid wound healing through their effects on increasing cellular migration and movements, but also typically promote metastasis in cancer. We conclude that FERM proteins play important roles in cellular migration, with markedly different outcomes in the context of cancer and wound healing.
authors.affiliation: Departments of Surgery and Wound Healing, Cardiff University School of Medicine, Heath Park, Cardiff CF14 4XW, UK.
authors.forename: David C
authors.initials: DC
authors.lastname: Bosanquet
authors.affiliation: Departments of Surgery and Wound Healing, Cardiff University School of Medicine, Heath Park, Cardiff CF14 4XW, UK.
authors.forename: Lin
authors.initials: L
authors.lastname: Ye
authors.affiliation: Departments of Surgery and Wound Healing, Cardiff University School of Medicine, Heath Park, Cardiff CF14 4XW, UK.
authors.forename: Keith G
authors.initials: KG
authors.lastname: Harding
authors.affiliation: Departments of Surgery and Wound Healing, Cardiff University School of Medicine, Heath Park, Cardiff CF14 4XW, UK.
authors.forename: Wen G
authors.initials: WG
authors.lastname: Jiang
mesh_terms: D008841:Actin Cytoskeleton / Q000737:chemistry / Q000378:metabolism; D002465:Cell Movement; D002471:Cell Transformation, Neoplastic / Q000235:genetics* / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000235:genetics* / Q000378:metabolism; D042783:Endothelial Cells / Q000166:cytology / Q000378:metabolism*; D005347:Fibroblasts / Q000166:cytology / Q000378:metabolism*; D005786:Gene Expression Regulation; D006801:Humans; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary; D015398:Signal Transduction; D014945:Wound Healing / Q000235:genetics*; D000099149:Ezrin
chemical_list: D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D020033:Protein Isoforms; D000099149:Ezrin; C478965:EPB41L4B protein, human; C028841:erythrocyte membrane band 4.1 protein; C071776:radixin