ArticleJournal of neurochemistry2011
Oxidative stress-induced oligomerization inhibits the activity of the non-receptor tyrosine phosphatase STEP61.
Article in Journal of neurochemistry, 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, 34 citations in OpenAlex.
- Regulating the Impact of Hypertension on Stroke: Therapeutic Potential of a Peptide Mimetic of Tyrosine Phosphatase STEP.Journal of the American Heart Association · 2026Article
- Disordered N-termini enhance the thermostability of SGNH-hydrolase family polyesterases.Protein science : a publication of the Protein Society · 2026Article
- Impairment of neuronal tyrosine phosphatase STEP worsens post-ischemic inflammation and brain injury under hypertensive condition.Journal of neuroinflammation · 2024Article
- Revving an Engine of Human Metabolism: Activity Enhancement of Triosephosphate Isomerase via Hemi-Phosphorylation.ACS chemical biology · 2022Article
- Regulation of Phosphorylated State of NMDA Receptor by STEPAntioxidants (Basel, Switzerland) · 2021Article
- Regulation of post-ischemic inflammatory response: A novel function of the neuronal tyrosine phosphatase STEP.Brain, behavior, and immunity · 2021Article
- Emerging neuroprotective strategies for the treatment of ischemic stroke: An overview of clinical and preclinical studies.Experimental neurology · 2021Review
- 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
- Higher levels of phosphorylated Y1472 on GluN2B subunits in the frontal cortex of aged mice are associated with good spatial reference memory, but not cognitive flexibility.Age (Dordrecht, Netherlands) · 2016Article
- Aging is associated with dimerization and inactivation of the brain-enriched tyrosine phosphatase STEP.Neurobiology of aging · 2016Article
- Molecular underpinnings of neurodegenerative disorders: striatal-enriched protein tyrosine phosphatase signaling and synaptic plasticity.F1000Research · 2016Review
- Disruption of striatal-enriched protein tyrosine phosphatase (STEP) function in neuropsychiatric disorders.Neuroscience research · 2014Review
- A common STEP in the synaptic pathology of diverse neuropsychiatric disorders.The Yale journal of biology and medicine · 2012Review
- Striatal-enriched protein tyrosine phosphatase in Alzheimer's disease.Advances in pharmacology (San Diego, Calif.) · 2012Review
- Therapeutic implications for striatal-enriched protein tyrosine phosphatase (STEP) in neuropsychiatric disorders.Pharmacological reviews · 2012Review
- Dephosphorylation of specific sites in the kinase-specificity sequence domain leads to ubiquitin-mediated degradation of the tyrosine phosphatase STEP.The Biochemical journal · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The neuron-specific tyrosine phosphatase STriatal Enriched Phosphatase (STEP) is emerging as an important mediator of glutamatergic transmission in the brain. STEP is also thought to be involved in the etiology of neurodegenerative disorders that are linked to oxidative stress such as Alzheimer's disease and cerebral ischemia. However, the mechanism by which oxidative stress can modulate STEP activity is still unclear. In this study, we have investigated whether dimerization may play a role in regulating the activity of STEP. Our findings show that STEP(61), the membrane associated isoform, can undergo homodimerization under basal conditions in neurons. Dimerization of STEP(61) involves intermolecular disulfide bond formation between two cysteine residues (Cys 65 and Cys 76 respectively) present in the hydrophobic region at the N-terminus specific to STEP(61). Oxidative stress induced by hydrogen peroxide leads to a significant increase in the formation of dimers and higher-order oligomers of STEP(61). Using two substrates, para-nitrophenylphosphate and extracellular-regulated kinase MAPK we further demonstrate that oligomerization leads to a significant reduction in its enzymatic activity.
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