The transcriptomes of hematopoietic stem and progenitor cells of human juvenile myelomonocytic leukemia patients and a zebrafish model for Noonan syndrome reveal a common inflammatory response, which may have a causal role in associated myeloproliferative neoplasm.

A molecular interpretation is provided for why some inhibitory immunoreceptors prefer to recruit SHP1 but others prefer SHP2.

Monitoring SHP2 phosphoproteome dynamics identifies new substrate sites and sites protected from dephosphorylation by its SH2 domains, highlighting distinct scaffolding and catalytic activities in effecting a transmembrane signaling response.

The stem cells of the postnatal muscle allow postnatal muscle growth and repair and withdraw from the cell cycle when the tyrosine phosphatase Ptpn11 (Shp2) is inhibited or mutated in mice.

A high-throughput method to profile tyrosine kinases and phosphotyrosine recognition domains reveals new rules for sequence specificity and maps the effects of mutations on the recognition of tyrosine phosphorylation sites.

The recruitment of SH2-containing proteins to Epidermal Growth Factor in cells happens more slowly than predicted by in vitro techniques.

The SHIP2 inositol phosphatase is an important upstream regulator of the Akt signaling pathway, which requires a catalytic core formed by the phosphatase domain tightly packed to a C2 domain for its function.

By binding to Fc gamma receptor IIb, amyloid beta induces a series of phosphorylation events that mediate the damaging effects of hyperphosphorylated tau proteins in Alzheimer's disease.

Comparative structural studies reveal how the cytoplasmic tails of Eph receptors can differentiate different downstream target proteins via highly specific SAM–SAM domain interactions.

Phosphorylation of the phosphatase SHP-1 by PKC-θ in natural killer (NK) cells induces SHP-1 inhibition, revealing a novel molecular pathway that sustains NK cell activation threshold.