Yu, Miao, Le, Shimin, Ammon, York-Christoph, Goult, Benjamin T, Akhmanova, Anna, Yan, Jie (2019) Force-dependent regulation of KANK1-talin complex at focal adhesions. Nano Letters, 19 (9). pp. 5982-5990. ISSN 1530-6992. (doi:10.1021/acs.nanolett.9b01732) (KAR id:75755)
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Official URL: http://dx.doi.org/10.1021/acs.nanolett.9b01732 |
Abstract
KANK proteins mediate cross-talk between dynamic microtubules and integrin- based adhesions to the extracellular matrix. KANKs interact with the integrin/actin-binding protein talin and with several components of microtubule-stabilizing cortical complexes. Because of actomyosin contractility, the talin−KANK complex is likely under mechanical force, and its mechanical stability is expected to be a critical determinant of KANK recruitment to focal adhesions. Here, we quantified the lifetime of the complex of the talin rod domain R7 and the KN domain of KANK1 under shear-force geometry and found that it can withstand forces for seconds to minutes over a physiological force range up to 10 pN. Complex stability measurements combined with cell biological experiments suggest that shear-force stretching promotes KANK1 localization to the periphery of focal adhesions. These results indicate that the talin−KANK1 complex is mechanically strong, enabling it to support the cross-talk between microtubule and actin cytoskeleton at focal adhesions.
Item Type: | Article |
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DOI/Identification number: | 10.1021/acs.nanolett.9b01732 |
Uncontrolled keywords: | talin, integrin, kank, adhesion, mechanobiology |
Subjects: | Q Science > QH Natural history > QH301 Biology |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Funders: | International Human Frontier Science Program Organization (https://ror.org/02ebx7v45) |
Depositing User: | Ben Goult |
Date Deposited: | 10 Aug 2019 17:11 UTC |
Last Modified: | 05 Nov 2024 12:40 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/75755 (The current URI for this page, for reference purposes) |
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