Regular ArticleNative Talin Is a Dumbbell-Shaped Homodimer When It Interacts with Actin
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Talin mechanotransduction in disease
2024, International Journal of Biochemistry and Cell BiologyA possible molecular mechanism for mechanotransduction at cellular focal adhesion complexes
2021, Biophysical ReportsThe Architecture of Talin1 Reveals an Autoinhibition Mechanism
2019, CellCitation Excerpt :We further tested if we could find talin dimers as a minor component in the molecular population. Sucrose-gradient centrifugation of talin-FL in the presence of a concomitant gradient of the cross-linker glutaraldehyde (GraFix) (Stark, 2010) showed a minor population of talin that migrated differently in solution as well as on SDS-PAGE (Figure 2C), suggesting the presence of a talin-FL dimer, in agreement with the previous report (Goldmann et al., 1994). In contrast, talin-ΔDD did not display the corresponding minor band and showed only a single monomeric population, indicating that DD is the only domain in talin that is capable of facilitating dimerization.
Gα<inf>13</inf> switch region 2 relieves talin autoinhibition to activate αiIbβ3 integrin
2016, Journal of Biological ChemistryCitation Excerpt :The limited proteolysis approach utilizes a small amount of protease that has little detectable effect on structurally stable proteins. The dimer fraction of platelet talin is reported to exhibit a dumbbell dimer conformation in an autoinhibited state (14, 16); thus, if Gα13SR2 perturbs this state, talin may become more vulnerable to limited proteolytic degradation. To validate this model, the dimeric fraction of platelet talin was purified and then pre-treated with Gα13SR2Pep or Gα13SR2RandomPep.
The talin dimer structure orientation is mechanically regulated
2014, Biophysical JournalCitation Excerpt :Talin has an integrin-binding head domain (18), and a rod domain consisting of 11 vinculin-binding sites (VBS) (19), at least two actin-binding sites (20), and a second integrin-binding site (21). The talin dimer, likely the orientation when bound to actin filaments (22), is antiparallel and likely in a Y-shape (23) or a dumbbell shape (20). Recent investigation suggests more variability in the shape of the talin dimer (24).
Mechanisms of talin-dependent integrin signaling and crosstalk
2014, Biochimica et Biophysica Acta - Biomembranes