Wang Y, Yeung Y G, Langdon W Y, Stanley E R
Department of Developmental, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
J Biol Chem. 1996 Jan 5;271(1):17-20. doi: 10.1074/jbc.271.1.17.
Early colony stimulating factor-1 (CSF-1)-induced changes in the behavior of p120c-cbl in mouse BAC1.2F5 macrophages were investigated. p120c-cbl is associated with Grb2 in the cytoplasm of unstimulated cells. Following a 1-min stimulation with CSF-1, p120c-cbl becomes tyrosine-phosphorylated and associates with tyrosine-phosphorylated Shc and an unknown phosphotyrosyl protein (pp80). Simultaneously, it is ubiquitinated and translocated to the membrane. By 10 min of stimulation, this c-Cbl exhibits substantially decreased tyrosine phosphorylation and is de-ubiquitinated and relocated in the cytosol. However, the association of p120c-cbl with Shc persists for at least 60 min. These data indicate that signaling via the CSF-1R involves the transient modification of p120c-cbl and its recruitment as a complex to membrane.
研究了早期集落刺激因子-1（CSF-1）诱导小鼠BAC1.2F5巨噬细胞中p120c-cbl行为的变化。在未受刺激的细胞胞质中，p120c-cbl与Grb2相关联。用CSF-1刺激1分钟后，p120c-cbl发生酪氨酸磷酸化，并与酪氨酸磷酸化的Shc和一种未知的磷酸酪氨酸蛋白（pp80）相关联。同时，它被泛素化并转运至细胞膜。刺激10分钟时，这种c-Cbl的酪氨酸磷酸化显著降低，去泛素化并重新定位于胞质溶胶中。然而，p120c-cbl与Shc的关联至少持续60分钟。这些数据表明，通过CSF-1R的信号传导涉及p120c-cbl的瞬时修饰及其作为复合物被募集至细胞膜。
