Membrane immunoglobulin: anti-immunoglobulin interactions mediate the phosphorylation of actin associated proteins in the B-lymphocyte.
Membrane immunoglobulin: anti-immunoglobulin interactions mediate the phosphorylation of actin associated proteins in the B-lymphocyte.
复制标题
膜免疫球蛋白：抗免疫球蛋白相互作用介导 B 淋巴细胞中肌动蛋白相关蛋白的磷酸化。
DOI：
10.1016/0024-3205(88)90089-6
复制
发表时间：
1988
期刊：
影响因子：
6.1
通讯作者：
Choi,YS
中科院分区：
文献类型：
--
作者：
Rosenspire,AJ;Choi,YS
The binding of membrane immunoglobulin (mIg) by anti-Ig anti-bodies is known to initiate a mitogenic signal in B lymphocytes. Because in many instances growth control appears to be correlated with phosphokinase activity, as well as with alterations in cytoskeletal architecture, we asked the question whether anti-bodies binding to mIg would also lead to the specific phosphorylation of lymphocyte actin-associated proteins. Utilizing a myosin affinity technique, we directly examined phosphoproteins that were associated with actin in the chicken B cell. We found that in a few instances the level of phosphorylation was indeed modulated by mIg:anti-Ig interactions. These actin-binding phosphoproteins may be important control elements in the lymphocyte cytoskeleton.
