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Regulation of T Cell Receptor Signaling by Tyrosine Phosphatase SYP Association with CTLA-4
The absence of CTLA-4 results in uncontrolled T cell proliferation. The T cell receptor-specific kinases FYN, LCK, and ZAP-70 as well as the RAS pathway were found to be activated in T cells ofExpand
SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases.
A mouse phosphotyrosine phosphatase containing two Src homology 2 (SH2) domains, Syp, was identified and was rapidly phosphorylated on tyrosine in PDGF- and EGF-stimulated cells. Expand
Shp-2 Tyrosine Phosphatase Functions as a Negative Regulator of the Interferon-Stimulated Jak/STAT Pathway
It is proposed that Shp-2 acts to promote cell growth and survival through two mechanisms, i.e., the stimulation of growth factor-initiated mitogenic pathways and the suppression of cytotoxic effect elicited by cytokines, such as IFNs. Expand
Protein-tyrosine Phosphatase Shp-2 Regulates Cell Spreading, Migration, and Focal Adhesion*
A unique role of the Shp-2 tyrosine phosphatase in cell motility is defined, which might guide the design of a new strategy for pharmaceutical interference of tumor metastasis. Expand
Neuronal Shp2 tyrosine phosphatase controls energy balance and metabolism.
It is suggested that a primary function of Shp2 in postmitotic forebrain neurons is to control energy balance and metabolism, and that this phosphatase is a critical signaling component of leptin receptor ObRb in the hypothalamus. Expand
Shp-2 tyrosine phosphatase: signaling one cell or many.
  • G. Feng
  • Biology, Medicine
  • Experimental cell research
  • 25 November 1999
The crystal structure of Shp-2 revealed an autoinhibitory mechanism of the catalytic activity by the N-terminal SH2 domain, which is an important molecule that integrates signals among various cytoplasmic pathways and may also couple intracellular and intercellular information flow. Expand
Involvement of the Src Homology 2-containing Tyrosine Phosphatase SHP-2 in Growth Hormone Signaling*
GH induced formation of a complex of tyrosine phosphoproteins including SHP-2, GHR, JAK2, and a glycoprotein with properties consistent with being a SIRP-α-like molecule, which implies a positive role for SHPs in GH signaling. Expand
Nuclear factor high‐mobility group box1 mediating the activation of toll‐like receptor 4 signaling in hepatocytes in the early stage of nonalcoholic fatty liver disease in mice
The notion thatTLR4/MyD88 signaling in liver parenchymal cells plays a pivotal role during the early progression of HFD‐induced NAFLD is supported, in which free HMGB1 served as a positive component mediating TLR4 activation. Expand
The 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp.
The interesting possibility that protein-tyrosine phosphatases contribute to the intracellular relay of biological signals originating from receptor tyrosine kinases such as the PDGFR is raised. Expand
Ptpn11/Shp2 acts as a tumor suppressor in hepatocellular carcinogenesis.
In contrast to the leukemogenic effect of dominant-active mutants, Ptpn11/Shp2 has a tumor-suppressor function in liver, and dramatically enhanced diethylnitrosamine-induced hepatocellular carcinoma development. Expand