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.
Publication Abstract from PubMed
Talin plays an important role in regulating integrin-mediated signaling. Talin function is autoinhibited by intramolecular interactions between the integrin-binding F3 domain and the autoinhibitory domain (R9). We determined the crystal structure of a triple-domain fragment, R7R8R9, which contains R9 and the RIAM (Rap1-interacting adaptor molecule) binding domain (R8). The structure reveals a crystallographic contact between R9 and a symmetrically related R8 domain, representing a homodimeric interaction in talin. Strikingly, we demonstrated that the alpha5 helix of R9 also interacts with the F3 domain, despite no interdomain contact involving the alpha5 helix in the crystal structure of an F2F3:R9 autoinhibitory complex reported previously. Mutations on the alpha5 helix significantly diminish the F3:R9 association and lead to elevated talin activity. Our results offer biochemical and functional evidence of the existence of a new talin autoinhibitory configuration, thus providing a more comprehensive understanding of talin autoinhibition, regulation, and quaternary structure assembly.
Structural and Functional Analysis of a Talin Triple-Domain Module Suggests an Alternative Talin Autoinhibitory Configuration.,Zhang H, Chang YC, Huang Q, Brennan ML, Wu J Structure. 2016 May 3;24(5):721-9. doi: 10.1016/j.str.2016.02.020. Epub 2016 Apr , 14. PMID:27150043[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhang H, Chang YC, Huang Q, Brennan ML, Wu J. Structural and Functional Analysis of a Talin Triple-Domain Module Suggests an Alternative Talin Autoinhibitory Configuration. Structure. 2016 May 3;24(5):721-9. doi: 10.1016/j.str.2016.02.020. Epub 2016 Apr , 14. PMID:27150043 doi:http://dx.doi.org/10.1016/j.str.2016.02.020
