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Casein kinase 2 promotes the TGF-モ–induced activation of メ-tubulin acetyltransferase 1 in fibroblasts cultured on a soft matrix
Eunae You1,# (Research worker), Jangho Jeong1,# (Research worker), Jieun Lee1 (Research worker), Seula Keum1 (Graduate student), Ye Eun Hwang1 (Graduate student), Jee-Hye Choi 1,# (Professor), Sangmyung Rhee 1,*,# (Professor)
1Department of Life Science, Chung-Ang University, Seoul, 06974, Republic of Korea
Abstract
Cell signals for growth factors depend on the mechanical properties of the extracellular matrix (ECM) surrounding the cells. Microtubule acetylation is involved in the transforming growth factor (TGF)-モ–induced myofibroblast differentiation in the soft ECM. However, the mechanism of activation of メ-tubulin acetyltransferase 1 (メ-TAT1), a major メ-tubulin acetyltransferase, in the soft ECM is not well defined. Here, we found that casein kinase 2 (CK2) is required for the TGF-モ–induced activation of メ-TAT1 that promotes microtubule acetylation in the soft matrix. Genetic mutation and pharmacological inhibition of CK2 catalytic activity specifically reduced microtubule acetylation in the cells cultured on a soft matrix rather than those cultured on a stiff matrix. Immunoprecipitation analysis showed that CK2メ, a catalytic subunit of CK2, directly bound to the C-terminal domain of メ-TAT1, and this interaction was more prominent in the cells cultured on the soft matrix. Moreover, the substitution of alanine with serine, the 236th amino acid located at the C-terminus, which contains the CK2-binding site of メ-TAT1, significantly abrogated the TGF-モ–induced microtubule acetylation in the soft matrix, indicating that the successful binding of CK2 and the C-terminus of メ-TAT1 led to the phosphorylation of serine at the 236th position of amino acids in メ-TAT1 and regulation of its catalytic activity. Taken together, our findings provide novel insights into the molecular mechanisms underlying the TGF-モ–induced activation of メ-TAT1 in a soft matrix.
Abstract, Accepted Manuscript(in press) [Submitted on January 30, 2022, Accepted on March 2, 2022]
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