Courtneidge S A, Fumagalli S
Differentiation Programme, European Molecular Biology Laboratory, Postfach 16.2209, Meyerhofstrasse 1, 69012 Heidelberg, Germany.
Trends Cell Biol. 1994 Oct;4(10):345-7. doi: 10.1016/0962-8924(94)90074-4.
During mitosis, the activity of the c-Src protein tyrosine kinase increases. The tyrosine phosphorylation of a 68 kDa protein (Sam68) also increases at this time, and recent studies have shown that Src and Sam68 interact. Sam68 is highly related to p62, a RasGAP-associated protein, and has homology to RNA-binding proteins. The relationship between p62 and Sam68, and their roles in Src signalling, need to be clarified, but these findings suggest that Src may participate in regulating RNA processing during the cell cycle.
在有丝分裂期间,c-Src蛋白酪氨酸激酶的活性增加。此时,一种68 kDa蛋白(Sam68)的酪氨酸磷酸化也增加,并且最近的研究表明Src与Sam68相互作用。Sam68与p62(一种RasGAP相关蛋白)高度相关,并且与RNA结合蛋白具有同源性。p62与Sam68之间的关系及其在Src信号传导中的作用需要阐明,但这些发现表明Src可能参与细胞周期中RNA加工的调控。