ArticleThe Biochemical journal2011
Dephosphorylation of specific sites in the kinase-specificity sequence domain leads to ubiquitin-mediated degradation of the tyrosine phosphatase STEP.
Article in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- The tyrosine phosphatase STEP is a developmental suppressor of synaptogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Regulating the Impact of Hypertension on Stroke: Therapeutic Potential of a Peptide Mimetic of Tyrosine Phosphatase STEP.Journal of the American Heart Association · 2026Article
- Impairment of neuronal tyrosine phosphatase STEP worsens post-ischemic inflammation and brain injury under hypertensive condition.Journal of neuroinflammation · 2024Article
- Fbxo45-mediated NP-STEPMolecular oncology · 2022Article
- Regulation of post-ischemic inflammatory response: A novel function of the neuronal tyrosine phosphatase STEP.Brain, behavior, and immunity · 2021Article
- The Implication of STEP in Synaptic Plasticity and Cognitive Impairments in Alzheimer's Disease and Other Neurological Disorders.Frontiers in cell and developmental biology · 2021Review
- Proteolytic Degradation of Hippocampal STEPMolecular neurobiology · 2019Article
- BDNF Induces Striatal-Enriched Protein Tyrosine Phosphatase 61 Degradation Through the Proteasome.Molecular neurobiology · 2016Article
- Aging is associated with dimerization and inactivation of the brain-enriched tyrosine phosphatase STEP.Neurobiology of aging · 2016Article
- 4E-BP1, a multifactor regulated multifunctional protein.Cell cycle (Georgetown, Tex.) · 2016Review
- Role of Striatal-Enriched Tyrosine Phosphatase in Neuronal Function.Neural plasticity · 2016Review
- Molecular underpinnings of neurodegenerative disorders: striatal-enriched protein tyrosine phosphatase signaling and synaptic plasticity.F1000Research · 2016Review
- Neuroprotective role of a brain-enriched tyrosine phosphatase, STEP, in focal cerebral ischemia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Genetic alterations associated with progression from pancreatic intraepithelial neoplasia to invasive pancreatic tumor.Gastroenterology · 2013Article
- In vitro stretch injury induces time- and severity-dependent alterations of STEP phosphorylation and proteolysis in neurons.Journal of neurotrauma · 2012Article
- Annexin A10 in human oral cancer: biomarker for tumoral growth via G1/S transition by targeting MAPK signaling pathways.PloS one · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
STEP (striatal-enriched phosphatase) is a non-receptor tyrosine phosphatase that is specifically expressed in the neurons of the central nervous system. STEP regulates the activity of several effector molecules involved in synaptic plasticity and neuronal cell survival, including MAPKs (mitogen-activated protein kinases), Src family kinases and NMDA (N-methyl-D-aspartic acid) receptors. The critical role of STEP in regulating these effectors requires that its activity be tightly regulated. Previous studies have demonstrated that the activity of STEP is regulated through reversible phosphorylation of a serine residue within the KIM (kinase-interacting motif), by cAMP-dependent PKA (protein kinase A). In the present paper we show that STEP is endogenously phosphorylated at two additional sites located within the KISs (kinase-specificity sequences). The basal activity of ERK (extracellular-signal-regulated kinase) and p38 MAPKs plays an important role in the phosphorylation of these two sites. Dephosphorylation of these two sites leads to polyubiquitination and proteolytic degradation of STEP. Conversely, the proteasome inhibitors MG-132 and epoxomicin can stabilize STEP. The active form of STEP is more susceptible to degradation than the inactive form. Taken together the results of the present paper establish that ubiquitin-dependent proteolysis could be a novel mechanism for irreversibly terminating the activity of STEP.
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