| Description | This entry represents the rod-segment of Talin-1/2. This domain interacts with its N-terminal FERM domain to mask its integrin-binding site and interferes with interactions between the FERM domain and the cellular membrane [ , ].Talin is a cytoskeletal protein that interacts with integrins and lipids. It forms an antiparallel homodimer with an N-terminal globular head and a larger C-terminal rod [ ]. The head domain contains a FERM (4.1, ezrin, radixin, moesin) domain, which has been implicated in both integrin and actin-binding. Binding of integrin beta cytoplasmic tails to the FERM domain has been found to induce integrin activation []. The rod domain also appears to mediate binding to both actin and integrins []. The C-terminal rod contains an I/LWEQ domain. It has been shown that the I/LWEQ domains from mouse talin and yeast Sla2p interact with F-actin [ ]. The domain has four conserved blocks, the name of the domain is derived from the initial conserved amino acid of each of the four blocks [].In vivo, talin has been shown to play a critical role in the formation of cell adhesions and regulation of integrin signalling in numerous species [ ]. Talin localises to some neuromuscular junction and sites of cell-cell adhesions, as well as to focal adhesions, sites of attachment to the substratum. | Name | Talin-1/2, rod-segment |
| Short Name | Talin1/2-RS | Type | Domain |
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