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目的探讨血管扩张刺激磷蛋白(VASP)及其丝氨酸157(p-VASP S157)和239(p-VASP S239)位点磷酸化与α-微管蛋白(α-Tubulin)之间的关系,明确VASP是一个新的微管相关蛋白。方法采用免疫荧光染色观察p-VASP S157、p-VASP S239和α-Tubulin在人宫颈癌上皮细胞HeLa的共定位;利用免疫共沉淀、微管沉淀和Western blot方法明确VASP及其不同位点磷酸化与α-Tubulin的结合情况。结果 VASP和p-VASP S157能够与α-Tubulin结合;p-VASP S239在细胞周期各个时期与α-Tubulin均无共定位关系。结论 VASP是一个新的微管相关蛋白,其丝氨酸157磷酸化与二者的结合相关。
Objective To investigate the relationship between VASP, phosphorylation of serine 157 (p-VASP S157) and 239 (p-VASP S239) and α-tubulin, Is a new microtubule-associated protein. Methods The co-localization of p-VASP S157, p-VASP S239 and α-Tubulin in human cervical epithelial cells HeLa was observed by immunofluorescence staining. The immunoprecipitation, microtubule precipitation and Western blotting were used to determine the relationship between VASP and different sites of phosphate The combination with α-Tubulin. Results VASP and p-VASP S157 could bind to α-Tubulin. P-VASP S239 had no colocalization with α-Tubulin at all stages of the cell cycle. Conclusion VASP is a novel microtubule-associated protein whose phosphorylation of serine 157 is related to the binding of the two proteins.