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Merck
CN
  • Different formins restrict localization of distinct tropomyosins on dorsal stress fibers in osteosarcoma cells.

Different formins restrict localization of distinct tropomyosins on dorsal stress fibers in osteosarcoma cells.

Cytoskeleton (Hoboken, N.J.) (2019-12-11)
Shuangshuang Zhao, Jinping Cai, Xin Zhang, Jie Cui, Yaming Jiu
摘要

Formins and tropomyosins (Tpms) are two central components of the microfilaments. Formins are involved in the nucleation and polymerization of actin filaments, and Tpms form along the actin stress fibers to regulate their dynamics. However, the correlation between formins and Tpms remains unclear. Here, we elucidated the function of distinct formins and their specific regulation to the subcellular-localization of Tpm isoforms on dorsal stress fibers in human osteosarcoma cells. Knockdown of individual formin isoform led to varied defects in actin stress fiber network, but did not affect the expression level of other formin isoforms and Tpms. Further investigation showed that different formins regulated distinct Tpm isoforms in decorating dorsal stress fibers. Specifically, DAAM1 and FHOD1 restricted the distal end expression of Tpm3.1; INF2 controlled the approximate localization of Tpm4.2; and Dia1 partially modulated the dorsal localization of Tpm1.6. Taken together, these data provide microscopy experimental evidence that different formins restrict the localization of distinct Tpm isoforms on dorsal actin stress fibers.

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Sigma-Aldrich
Anti-MYO18B antibody produced in rabbit, affinity isolated antibody, buffered aqueous glycerol solution
Sigma-Aldrich
Anti-FHOD1 antibody produced in rabbit, ~1.0 mg/mL, affinity isolated antibody
Sigma-Aldrich
Anti-INF2 antibody produced in mouse, purified immunoglobulin, buffered aqueous solution
Sigma-Aldrich
Anti-DAAM1 antibody produced in rabbit, affinity isolated antibody