Structural highlights
Function
[TLN1_MOUSE] Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
FERM domains are found in a diverse superfamily of signaling and adaptor proteins at membrane interfaces. They typically consist of three separately folded domains (F1, F2, F3) in a compact cloverleaf structure. The crystal structure of the N-terminal head of the integrin-associated cytoskeletal protein talin reported here reveals a novel FERM domain with a linear domain arrangement, plus an additional domain F0 packed against F1. While F3 binds beta-integrin tails, basic residues in F1 and F2 are required for membrane association and for integrin activation. We show that these same residues are also required for cell spreading and focal adhesion assembly in cells. We suggest that the extended conformation of the talin head allows simultaneous binding to integrins via F3 and to PtdIns(4,5)P2-enriched microdomains via basic residues distributed along one surface of the talin head, and that these multiple interactions are required to stabilize integrins in the activated state.
The Structure of the talin head reveals a novel extended conformation of the FERM domain.,Elliott PR, Goult BT, Kopp PM, Bate N, Grossmann JG, Roberts GC, Critchley DR, Barsukov IL Structure. 2010 Oct 13;18(10):1289-99. PMID:20947018[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Elliott PR, Goult BT, Kopp PM, Bate N, Grossmann JG, Roberts GC, Critchley DR, Barsukov IL. The Structure of the talin head reveals a novel extended conformation of the FERM domain. Structure. 2010 Oct 13;18(10):1289-99. PMID:20947018 doi:10.1016/j.str.2010.07.011
