دورية أكاديمية
The actin binding sites of talin have both distinct and complementary roles in cell-ECM adhesion.
| العنوان: | The actin binding sites of talin have both distinct and complementary roles in cell-ECM adhesion. |
|---|---|
| المؤلفون: | Camp D; Department of Cellular and Physiological Sciences, University of British Columbia, Vancouver, British Columbia, Canada., Venkatesh B; Department of Cellular and Physiological Sciences, University of British Columbia, Vancouver, British Columbia, Canada., Solianova V; Department of Cellular and Physiological Sciences, University of British Columbia, Vancouver, British Columbia, Canada., Varela L; School of Biosciences, University of Kent, Canterbury, Kent, United Kingdom., Goult BT; School of Biosciences, University of Kent, Canterbury, Kent, United Kingdom.; Department of Biochemistry, Cell & Systems Biology, Institute of Systems, Molecular & Integrative Biology, University of Liverpool, Crown Street, Liverpool L69 7ZB, United Kingdom., Tanentzapf G; Department of Cellular and Physiological Sciences, University of British Columbia, Vancouver, British Columbia, Canada. |
| المصدر: | PLoS genetics [PLoS Genet] 2024 Apr 25; Vol. 20 (4), pp. e1011224. Date of Electronic Publication: 2024 Apr 25 (Print Publication: 2024). |
| نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Public Library of Science Country of Publication: United States NLM ID: 101239074 Publication Model: eCollection Cited Medium: Internet ISSN: 1553-7404 (Electronic) Linking ISSN: 15537390 NLM ISO Abbreviation: PLoS Genet Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: San Francisco, CA : Public Library of Science, c2005- |
| مواضيع طبية MeSH: | Actins*/metabolism , Actins*/genetics , Cell Adhesion*/genetics , Extracellular Matrix*/metabolism , Talin*/metabolism , Talin*/genetics, Animals ; Actin Cytoskeleton/metabolism ; Actin Cytoskeleton/genetics ; Binding Sites ; Cytoskeleton/metabolism ; Cytoskeleton/genetics ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Integrins/metabolism ; Integrins/genetics ; Mutation ; Protein Binding |
| مستخلص: | Cell adhesion requires linkage of transmembrane receptors to the cytoskeleton through intermediary linker proteins. Integrin-based adhesion to the extracellular matrix (ECM) involves large adhesion complexes that contain multiple cytoskeletal adapters that connect to the actin cytoskeleton. Many of these adapters, including the essential cytoskeletal linker Talin, have been shown to contain multiple actin-binding sites (ABSs) within a single protein. To investigate the possible role of having such a variety of ways of linking integrins to the cytoskeleton, we generated mutations in multiple actin binding sites in Drosophila talin. Using this approach, we have been able to show that different actin-binding sites in talin have both unique and complementary roles in integrin-mediated adhesion. Specifically, mutations in either the C-terminal ABS3 or the centrally located ABS2 result in lethality showing that they have unique and non-redundant function in some contexts. On the other hand, flies simultaneously expressing both the ABS2 and ABS3 mutants exhibit a milder phenotype than either mutant by itself, suggesting overlap in function in other contexts. Detailed phenotypic analysis of ABS mutants elucidated the unique roles of the talin ABSs during embryonic development as well as provided support for the hypothesis that talin acts as a dimer in in vivo contexts. Overall, our work highlights how the ability of adhesion complexes to link to the cytoskeleton in multiple ways provides redundancy, and consequently robustness, but also allows a capacity for functional specialization. Competing Interests: The authors have declared that no competing interests exist. (Copyright: © 2024 Camp et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.) |
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| معلومات مُعتمدة: | P40 OD018537 United States OD NIH HHS |
| المشرفين على المادة: | 0 (Actins) 0 (Drosophila Proteins) 0 (Integrins) 0 (Talin) |
| تواريخ الأحداث: | Date Created: 20240425 Date Completed: 20240507 Latest Revision: 20240603 |
| رمز التحديث: | 20240603 |
| مُعرف محوري في PubMed: | PMC11075885 |
| DOI: | 10.1371/journal.pgen.1011224 |
| PMID: | 38662776 |
| قاعدة البيانات: | MEDLINE |
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