Institute of Anatomy and Cell Biology, Justus-Liebig-University, 35392 Giessen, Germany.
Institute of Pathology, Justus-Liebig-University, 35392 Giessen, Germany.
Int J Mol Sci. 2018 Oct 22;19(10):3282. doi: 10.3390/ijms19103282.
The protein tyrosine phosphatase interacting protein 51 (PTPIP51) regulates and interconnects signaling pathways, such as the mitogen-activated protein kinase (MAPK) pathway and an abundance of different others, e.g., Akt signaling, NF-κB signaling, and the communication between different cell organelles. PTPIP51 acts as a scaffold protein for signaling proteins, e.g., Raf-1, epidermal growth factor receptor (EGFR), human epidermal growth factor receptor 2 (Her2), as well as for other scaffold proteins, e.g., 14-3-3 proteins. These interactions are governed by the phosphorylation of serine and tyrosine residues of PTPIP51. The phosphorylation status is finely tuned by receptor tyrosine kinases (EGFR, Her2), non-receptor tyrosine kinases (c-Src) and the phosphatase protein tyrosine phosphatase 1B (PTP1B). This review addresses various diseases which display at least one alteration in these enzymes regulating PTPIP51-interactions. The objective of this review is to summarize the knowledge of the MAPK-related interactome of PTPIP51 for several tumor entities and metabolic disorders.
蛋白酪氨酸磷酸酶相互作用蛋白 51（PTPIP51）调节和相互连接信号通路，如丝裂原活化蛋白激酶（MAPK）通路和许多其他通路，如 Akt 信号通路、NF-κB 信号通路以及不同细胞细胞器之间的通讯。PTPIP51 作为信号蛋白的支架蛋白，如 Raf-1、表皮生长因子受体（EGFR）、人表皮生长因子受体 2（Her2），以及其他支架蛋白，如 14-3-3 蛋白。这些相互作用受 PTPIP51 丝氨酸和酪氨酸残基的磷酸化调控。磷酸化状态由受体酪氨酸激酶（EGFR、Her2）、非受体酪氨酸激酶（c-Src）和磷酸酶蛋白酪氨酸磷酸酶 1B（PTP1B）精细调节。本综述讨论了至少在这些调节 PTPIP51 相互作用的酶中存在一种改变的各种疾病。本综述的目的是总结 PTPIP51 与几种肿瘤实体和代谢紊乱相关的 MAPK 相关相互作用组的知识。
