Abstract
Abstract Cellular responses to mechanical stimuli play an imperative role in the regulation of physiological and pathological functions. Unlike other integrin-mediated adhesion proteins, the force transmission mechanism of tensin1 is not well understood. In this study, we describe the development and visualization of a tensin1 tension sensor. A signal from this sensor indicates that tensin1 is under greater tension at peripheral adhesions than at central adhesions, and that it is controlled by actomyosin in fibroblasts. In a bidirectional manner, tension in tensin1 is regulated by focal adhesion kinase (FAK) activity. Our findings demonstrate that tensin1 is capable of sensing the extracellular matrix through alterations in the tension it receives from the extracellular matrix. Furthermore, tensin1 depletion increases the tension of talin1, but the absence of talin1 decreases the tension applied to tensin1. These results indicate that tensin1 is complementary and dependent on the tension received by talin1. Overall, our data, together with the prognosis following tensin1 expression in colorectal and urothelial cancer, elucidate the tension-receiving function of tensin1 and highlight the necessity of tensin1-mediated mechanotransduction studies. Citation Format: Yoon-Kwan Jang, Jung-Soo Suh, Gyuho Choi, Sanghyun Ahn, Ki Seok Han, EunHye Kim, Yerim Lee, Xiaoqi Hu, Eunbae Hwang, Tae-Jin Kim. Tensin1 tension sensor reveals novel features associated with actomyosin, focal adhesion dynamics, and mechanosensitivity [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2023; Part 1 (Regular and Invited Abstracts); 2023 Apr 14-19; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2023;83(7_Suppl):Abstract nr 5816.
Published Version
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