Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/26739
Title: Central region of talin has a unique fold that binds vinculin and actin.
Authors: Gingras, AR
Bate, N
Goult, BT
Patel, B
Kopp, PM
Emsley, J
Barsukov, IL
Roberts, GC
Critchley, DR
First Published: 17-Sep-2010
Citation: J BIOL CHEM, 2010, 285 (38), pp. 29577-29587
Abstract: Talin is an adaptor protein that couples integrins to F-actin. Structural studies show that the N-terminal talin head contains an atypical FERM domain, whereas the N- and C-terminal parts of the talin rod include a series of α-helical bundles. However, determining the structure of the central part of the rod has proved problematic. Residues 1359-1659 are homologous to the MESDc1 gene product, and we therefore expressed this region of talin in Escherichia coli. The crystal structure shows a unique fold comprised of a 5- and 4-helix bundle. The 5-helix bundle is composed of nonsequential helices due to insertion of the 4-helix bundle into the loop at the C terminus of helix α3. The linker connecting the bundles forms a two-stranded anti-parallel β-sheet likely limiting the relative movement of the two bundles. Because the 5-helix bundle contains the N and C termini of this module, we propose that it is linked by short loops to adjacent bundles, whereas the 4-helix bundle protrudes from the rod. This suggests the 4-helix bundle has a unique role, and its pI (7.8) is higher than other rod domains. Both helical bundles contain vinculin-binding sites but that in the isolated 5-helix bundle is cryptic, whereas that in the isolated 4-helix bundle is constitutively active. In contrast, both bundles are required for actin binding. Finally, we show that the MESDc1 protein, which is predicted to have a similar fold, is a novel actin-binding protein.
DOI Link: 10.1074/jbc.M109.095455
eISSN: 1083-351X
Links: http://hdl.handle.net/2381/26739
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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