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BDNF Induces Striatal-Enriched Protein Tyrosine Phosphatase 61 Degradation Through the Proteasome

Molecular neurobiology, 2016-08, Vol.53 (6), p.4261-4273 [Peer Reviewed Journal]

Springer Science+Business Media New York 2015 ;Springer Science+Business Media New York 2016 ;ISSN: 0893-7648 ;EISSN: 1559-1182 ;DOI: 10.1007/s12035-015-9335-7 ;PMID: 26223799

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Title:
BDNF Induces Striatal-Enriched Protein Tyrosine Phosphatase 61 Degradation Through the Proteasome
Author: Saavedra, Ana ; Puigdellívol, Mar ; Tyebji, Shiraz ; Kurup, Pradeep ; Xu, Jian ; Ginés, Silvia ; Alberch, Jordi ; Lombroso, Paul J. ; Pérez-Navarro, Esther
Subjects: Animals ; Biomedical and Life Sciences ; Biomedicine ; Brain ; Brain-Derived Neurotrophic Factor - pharmacology ; Cell Biology ; Cerebral Cortex - cytology ; Extracellular Signal-Regulated MAP Kinases - metabolism ; Hippocampus - cytology ; Kinases ; Membrane Potentials - drug effects ; Mice ; Molecular biology ; Neostriatum - metabolism ; Nerve Growth Factor - pharmacology ; Neurobiology ; Neurology ; Neurons - metabolism ; Neurosciences ; Neurotrophin 3 - pharmacology ; Phospholipase C gamma - metabolism ; Phosphorylation - drug effects ; Proteasome Endopeptidase Complex - metabolism ; Protein Tyrosine Phosphatases, Non-Receptor - metabolism ; Proteins ; Proteolysis - drug effects ; Receptors, N-Methyl-D-Aspartate - metabolism ; Ubiquitination - drug effects
Is Part Of: Molecular neurobiology, 2016-08, Vol.53 (6), p.4261-4273
Description: Brain-derived neurotrophic factor (BDNF) promotes synaptic strengthening through the regulation of kinase and phosphatase activity. Conversely, striatal-enriched protein tyrosine phosphatase (STEP) opposes synaptic strengthening through inactivation or internalization of signaling molecules. Here, we investigated whether BDNF regulates STEP levels/activity. BDNF induced a reduction of STEP 61 levels in primary cortical neurons, an effect that was prevented by inhibition of tyrosine kinases, phospholipase C gamma, or the ubiquitin-proteasome system (UPS). The levels of pGluN2B Tyr1472 and pERK1/2 Thr202/Tyr204 , two STEP substrates, increased in BDNF-treated cultures, and blockade of the UPS prevented STEP 61 degradation and reduced BDNF-induced GluN2B and ERK1/2 phosphorylation. Moreover, brief or sustained cell depolarization reduced STEP 61 levels in cortical neurons by different mechanisms. BDNF also promoted UPS-mediated STEP 61 degradation in cultured striatal and hippocampal neurons. In contrast, nerve growth factor and neurotrophin-3 had no effect on STEP 61 levels. Our results thus indicate that STEP 61 degradation is an important event in BDNF-mediated effects.
Publisher: New York: Springer US
Language: English
Identifier: ISSN: 0893-7648
EISSN: 1559-1182
DOI: 10.1007/s12035-015-9335-7
PMID: 26223799
Source: ProQuest One Psychology
MEDLINE
ProQuest Central

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BDNF Induces Striatal-Enriched Protein Tyrosine Phosphatase 61 Degradation Through the Proteasome

Springer Science+Business Media New York 2015 ;Springer Science+Business Media New York 2016 ;ISSN: 0893-7648 ;EISSN: 1559-1182 ;DOI: 10.1007/s12035-015-9335-7 ;PMID: 26223799

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