脱磷
磷酸酶
磷酸化
蛋白质酪氨酸磷酸酶
生物
信号转导
细胞生物学
锡克
细胞信号
信号蛋白
酪氨酸激酶
作者
Alexander Y. Tsygankov
标识
DOI:10.1016/j.cellsig.2019.109424
摘要
Two members of the UBASH3/STS/TULA family exhibit a unique protein domain structure, which includes a histidine phosphatase domain, and play a key role in regulating cellular signaling. UBASH3A/STS-2/TULA is mostly a lymphoid protein, while UBASH3B/STS-1/TULA-2 is expressed ubiquitously. Dephosphorylation of tyrosine-phosphorylated proteins by TULA-2 and, probably to a lesser extent, by TULA critically contribute to the molecular basis of their regulatory effect. The notable differences between the effects of the two family members on cellular signaling and activation are likely to be linked to the difference between their specific enzymatic activities. However, these differences might also be related to the functions of their domains other than the phosphatase domain and independent of their phosphatase activity. The down-regulation of the Syk/Zap-70-mediated signaling, which to-date appears to be the best-studied regulatory effect of TULA family, is discussed in detail in this publication.
科研通智能强力驱动
Strongly Powered by AbleSci AI