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Involvement of a calcineurin/ inhibitor-1 phosphatase cascade in hippocampal long-term depression
A signalling pathway in which calcineurin dephosphorylates and inactivates inhibitor-1 increases PP1 activity and contributes to the generation of LTD, which is suggested to be an activity-dependent decrease in synaptic efficacy.
A signalling pathway controlling c-Myc degradation that impacts oncogenic transformation of human cells
It is shown that Ser 62 is dephosphorylated by protein phosphatase 2A (PP2A) before ubiquitination of c-Myc, and that PP2A activity is regulated by the Pin1 prolyl isomerase, resulting in c- myc stabilization.
Structural and biophysical studies of PCSK9 and its mutants linked to familial hypercholesterolemia
The structure of human PCSK9 shows the subtilisin-like catalytic site blocked by the prodomain in a noncovalent complex and inaccessible to exogenous ligands, and that the C-terminal domain has a novel fold.
Gating of CaMKII by cAMP-regulated protein phosphatase activity during LTP.
The cAMP pathway uses PP1 to gate CaMKII signaling in LTP, and the blockade of LTP by a Ca MKII inhibitor was not overcome by thiophosphorylated inhibitor-1.
From promiscuity to precision: protein phosphatases get a makeover.
Targeted disruption of the mouse NHERF-1 gene promotes internalization of proximal tubule sodium-phosphate cotransporter type IIa and renal phosphate wasting
- S. Shenolikar, J. Voltz, C. Minkoff, J. Wade, E. Weinman
- BiologyProceedings of the National Academy of Sciences…
- 8 August 2002
Phosphate wasting seen in the NHERF-1(−/−) null mice provided a new experimental system for defining the role of PDZ adapters in the hormonal control of ion transport and renal disease.
Molecular memory by reversible translocation of calcium/calmodulin-dependent protein kinase II
This work shows that a regulator of synaptic plasticity, calcium/calmodulin-dependent protein kinase IIα (CaMKII), sequentially translocates to postsynaptic sites, undergoes autophosphorylation and gets trapped for several minutes until its dissociation is induced by secondary autoph phosphorylated and phosphatase 1 action.
Protein phosphatases: recent progress.
Characterization of a protein cofactor that mediates protein kinase A regulation of the renal brush border membrane Na(+)-H+ exchanger.
The present experiments detail the structure of the NHE-RF protein as determined from molecular cloning studies and locate potential phosphorylation sites for protein kinase A in the mRNA for the protein, which is expressed in kidney, proximal small intestine, and liver.
Protein serine/threonine phosphatases--new avenues for cell regulation.
- S. Shenolikar
- BiologyAnnual Review of Cell Biology