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.

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

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.

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.

The tandem SH2 domains of Spt6 use novel mechanisms to bind unexpected phosphorylated serine and threonine residues in the RNA polymerase II linker to recruit Spt6 to sites of transcription and maintain repressive chromatin.

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.

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

Crk proteins are critical mediators of FGF signaling to control cell shape changes.

Based on its nucleotide-bound state, the Chd1 chromatin remodeler can locally alter DNA twist on the nucleosome, which either pulls in or expels ~1 bp of DNA at the internal SHL2 binding site.

Chronic engagement of Natural killer cell inhibitory receptors by MHC-I molecules maintains a high activity of the mTOR pathway allowing subsequent amplification of signaling through activating receptors upon acute stimulation.