HCO3–-sensitive regulation of endothelium-dependent vasorelaxation by receptor-type tyrosine-protein phosphatase RPTPγ provides a novel mechanism for acid-base-mediated coordination of cerebrovascular perfusion during increased local metabolism and for protection against ischemia.
Presynaptic adhesion molecule PTPσ in the hippocampus regulates postsynaptic NMDA receptor function and behavioral novelty recognition through mechanisms independent of their trans-synaptic binding partners.
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.
Plasticity arising from autocatalytic receptor activation coexists with robustness in ligand responsiveness only by differential endosomal sorting of spontaneous and ligand-activated EGFR as distinct molecular states.
Systematic proteomic approaches identify several cell junction regulators as substrates for the homophilic receptor tyrosine phosphatase PTPRK and implicate its pseudophosphatase domain in substrate recognition.
Leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-RPTPs) are precisely localized to synaptic appositions, but do not control the assembly and function of the presynaptic nerve terminal.
Two receptor tyrosine phosphatases having overlapping function for the determination of the final axon stabilizing layer is encoded for their cumulative cytoplasmic activity and ligand specificity in the visual system.