| Description | Plakins are a family of seven cytoskeletal cross-linker proteins (microtubule-actin crosslinking factor 1 (MACF), bullous pemphigoid antigen (BPAG1) desmoplakin, envoplakin, periplakin, plectin, epiplakin) that network the major filaments of the cytoskeleton [ ].Plakins have been shown to play a diverse range of biological roles. MACF1 and BPAG1 perform cross-linking functions between actin and microtubules and have been shown to play roles in cell migration and microtubule organisation, while plectin cross-links intermediate filaments to microtubules [ ].Desmoplakin, envoplakin, periplakin and epiplakin are predominately involved in intermediate filament binding. They have been found to play a prominent role in the development of the cornified envelop, in the epidermis. Additional roles have been demonstrated for desmoplakin in myocardium morphogenesis, epidermis development, keratinocyte differentiation, and, along with MACF1, wound healing. Plakins have also been found to be involved in intracellular signalling cascades [ ].Plakin family members are built from combinations of the following modules: a calponin-type actin-binding domain (ABD); a plakin domain harbouring several α-helical bundles; a heptad-repeat-containing coiled-coil rod domain (CC-rod); a plakin-repeat domain (PRD) generally thought to have intermediate filament (IF)-binding properties, a function that in some cases requires an associated linker (L) subdomain; a spectrin repeat (SR)-containing rod domain; two EF-hand calcium-binding motifs; a Gas2-homology region called the GAR domain; and a domain containing GSR (Gly-Ser-Arg) repeats [ ].This family represents proteins found predominantly in metazoans. | Name | Plakin |
| Short Name | Plakin | Type | Family |
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