Tyrosine-protein phosphatase non-receptor type 2(PTPN2), an important member of the protein tyrosine phosphatase family, can regulate various signaling pathways and biological processes by dephosphorylating receptor protein tyrosine kinases. Accumulating
Xiao-Er Tang +2 more
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Tyrosine phosphorylation controls brassinosteroid receptor activation by triggering membrane release of its kinase inhibitor [PDF]
Receptor tyrosine kinases control many critical processes in metazoans, but these enzymes appear to be absent in plants. Recently, two Arabidopsis receptor kinases-BRASSINOSTEROID INSENSITIVE 1 (BRI1) and BRI1-ASSOCIATED KINASE1 (BAK1), the ...
Belkhadir, Youssef +6 more
core +4 more sources
Tyrosine 402 phosphorylation of Pyk2 is involved in ionomycin-induced neurotransmitter release. [PDF]
Protein tyrosine kinases, which are highly expressed in the central nervous system, are implicated in many neural processes. However, the relationship between protein tyrosine kinases and neurotransmitter release remains unknown.
Zhao Zhang +9 more
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Receptor Protein Tyrosine Kinases and Phosphatases
It is clear that the number of receptor PTKs and PTPs encoded by a typical vertebrate genome is rather large. Although the signal pathways activated by the receptor PTKs may in many cases be common, specificity is provided by the ligand-binding domain and the availability of ligand.
T, Hunter +4 more
openaire +2 more sources
In metazoans, receptor kinases control many essential processes related to growth and development and response to the environment. The receptor kinases in plants and animals are structurally similar but evolutionarily distinct and thus while most animal ...
Man-Ho eOh +3 more
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Targeting RTK signaling pathways in cancer [PDF]
The RAS/MAP kinase and the RAS/PI3K/AKT pathways play a key role in the regulation of proliferation, differentiation and survival. The induction of these pathways depends on Receptor Tyrosine Kinases (RTKs) that are activated upon ligand binding.
Regad, T
core +1 more source
Grb2 binding induces phosphorylation-independent activation of Shp2
Lin et al. investigate the interactions between adaptor protein, Grb2, and the ubiquitously expressed protein tyrosine phosphatase, Shp2. They find that monomeric Grb2 can activate Shp2 and its downstream signalling in the absence of up-regulation of ...
Chi-Chuan Lin +5 more
doaj +1 more source
Targeting Brutons Tyrosine Kinase in Chronic Lymphocytic Leukemia at the Crossroad between Intrinsic and Extrinsic Pro-survival Signals [PDF]
Chemo immunotherapies for chronic lymphocytic leukemia (CLL) showed a positive impact on clinical outcome, but many patients relapsed or become refractory to the available treatments.
Facco, Monica +7 more
core +1 more source
Complex formation of EphB1/Nck/Caskin1 leads to tyrosine phosphorylation and structural changes of the Caskin1 SH3 domain. [PDF]
Scaffold proteins have an important role in the regulation of signal propagation. These proteins do not possess any enzymatic activity but can contribute to the formation of multiprotein complexes.
Balázs Annamária +6 more
core +2 more sources
Activation of tyrosine kinases by mutation of the gatekeeper threonine. [PDF]
Protein kinases targeted by small-molecule inhibitors develop resistance through mutation of the gatekeeper threonine residue of the active site. Here we show that the gatekeeper mutation in the cellular forms of c-ABL, c-SRC, platelet-derived growth ...
Azam, Mohammad +4 more
core +1 more source

