Rankin S, Morii N, Narumiya S, Rozengurt E
Imperial Cancer Research Fund, London, UK.
FEBS Lett. 1994 Nov 14;354(3):315-9. doi: 10.1016/0014-5793(94)01148-6.
In this study we examined the role of rho p21 in neuropeptide-stimulated tyrosine phosphorylation. Intact Swiss 3T3 cells were treated with the Clostridium botulinum C3 exoenzyme which specifically ADP ribosylates and inactivates rho p21. C3 exoenzyme treatment of cells caused a marked decrease in both bombesin- and endothelin-stimulated tyrosine phosphorylation of multiple proteins, including p125 focal adhesion kinase (FAK) and paxillin. Our results suggest that rho p21 is a component of the signal transduction pathway linking seven transmembrane domain receptors with tyrosine phosphorylation and cytoskeletal events.
在本研究中，我们检测了rho p21在神经肽刺激的酪氨酸磷酸化中的作用。用肉毒杆菌C3外毒素处理完整的瑞士3T3细胞，该毒素能特异性地使rho p21发生ADP核糖基化并使其失活。用C3外毒素处理细胞导致多种蛋白（包括p125粘着斑激酶（FAK）和桩蛋白）在蛙皮素和内皮素刺激下的酪氨酸磷酸化显著降低。我们的结果表明，rho p21是将七跨膜结构域受体与酪氨酸磷酸化及细胞骨架事件联系起来的信号转导途径的一个组成部分。
