Tropomyosin 3.5 protects F-actin networks required for tissue biomechanical properties
Autor: | Catherine Cheng, Roberta B. Nowak, Sondip K. Biswas, Michael B. Amadeo, Velia M. Fowler, Woo-Kuen Lo |
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Rok vydání: | 2018 |
Předmět: |
Gene isoform
0301 basic medicine Cell Tropomyosin macromolecular substances Actinin Tropomyosin 3 law.invention Mice 03 medical and health sciences In vivo law Lens Crystalline medicine Animals Spectrin education Actin education.field_of_study Mechanical load biology Chemistry Cell Differentiation Cell Biology Actins Lens Fiber Lens (optics) medicine.anatomical_structure 030104 developmental biology Fimbrin biology.protein Biophysics Tropomodulin Research Article |
Zdroj: | Journal of Cell Science. |
ISSN: | 1477-9137 0021-9533 |
DOI: | 10.1242/jcs.222042 |
Popis: | Tropomyosins (Tpms) stabilize F-actin and regulate interactions with other actin-binding proteins. The eye lens changes shape in order to fine focus light to transmit a clear image, and thus lens organ function is tied to its biomechanical properties, presenting an opportunity to study Tpm functions in tissue mechanics. The major mouse lens Tpm is Tpm3.5 (TM5NM5), a previously unstudied isoform. Decreased levels of Tpm3.5 lead to softer and less mechanically resilient lenses that are unable to resume their original shape after compression. While cell organization and morphology appear unaffected, Tmod1 dissociates from the membrane in Tpm3.5-deficient lens fiber cells resulting in reorganization of the spectrin-F-actin and α-actinin-F-actin networks at the membrane. These rearranged F-actin networks appear to be less able to support mechanical load and resilience leading to an overall change in tissue mechanical properties. This is the firstin vivoevidence that Tpm is essential for cell biomechanical stability in a load-bearing non-muscle tissue and indicates that Tpm3.5 protects mechanically stable, load-bearing F-actinin vivo.SummaryTropomyosin 3.5 stabilizes F-actin in eye lens fiber cells and promotes normal tissue biomechanical properties. Tpm3.5 deficiency leads to F-actin network rearrangements and decreased lens stiffness and resilience. |
Databáze: | OpenAIRE |
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