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首页> 外文期刊>American Journal of Physiology >Tropomyosin interacts with phosphorylated HSP27 in agonist-induced contraction of smooth muscle.
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Tropomyosin interacts with phosphorylated HSP27 in agonist-induced contraction of smooth muscle.

机译：Tropomyosin在激动剂诱导的平滑肌收缩中与磷酸化的HSP27相互作用。

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摘要

Displacement of the contractile protein tropomyosin from actin filament exposes the myosin-binding sites on actin, resulting in actin-myosin interaction and muscle contraction. The objective of the present study was to better understand the interaction of tropomyosin with heat shock protein (HSP)27 in contraction of smooth muscle cells of the colon. We investigated the possibility of a direct protein-protein interaction of tropomyosin with HSP27 and the role of phosphorylated HSP27 in this interaction. Immunoprecipitation studies on rabbit smooth muscle cells indicate that upon acetylcholine-induced contraction tropomyosin shows increased association with HSP27 phosphorylated at Ser82 and Ser78. Transfection of smooth muscle cells with HSP27 phosphorylation mutants indicated that the association of tropomyosin with HSP27 could be affected by HSP27 phosphorylation. In vitro binding studies with glutathione S-transferase (GST)-tagged HSP27 mutant proteins show that tropomyosin has greater direct interaction to phosphomimic HSP27 mutant compared with wild-type and nonphosphomimic HSP27. Our data suggest that, in response to a contractile agonist, HSP27 undergoes a rapid phosphorylation that may strengthen its interaction with tropomyosin.
机译：肌动蛋白丝中收缩蛋白原肌球蛋白的置换暴露了肌动蛋白上的肌球蛋白结合位点，导致肌动蛋白-肌球蛋白相互作用和肌肉收缩。本研究的目的是更好地了解原肌球蛋白与热休克蛋白（HSP）27在结肠平滑肌细胞收缩中的相互作用。我们调查了原肌球蛋白与HSP27直接蛋白相互作用的可能性以及磷酸化HSP27在这种相互作用中的作用。对兔平滑肌细胞的免疫沉淀研究表明，乙酰胆碱引起的收缩原肌球蛋白显示与在Ser82和Ser78磷酸化的HSP27的缔合增加。 HSP27磷酸化突变体对平滑肌细胞的转染表明原肌球蛋白与HSP27的缔合可能受HSP27磷酸化的影响。带有谷胱甘肽S-转移酶（GST）标签的HSP27突变蛋白的体外结合研究表明，与野生型和非磷酸化HSP27相比，原肌球蛋白与磷酸化HSP27突变体具有更大的直接相互作用。我们的数据表明，响应收缩性激动剂，HSP27发生快速磷酸化，这可能会增强其与原肌球蛋白的相互作用。

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