MODULATION OF PHOSPHORYLATION OF NEURONAL CYTOSKELETAL PROTEINS BY NEURONAL DEPOLARIZATION

Citation
M. Mata et al., MODULATION OF PHOSPHORYLATION OF NEURONAL CYTOSKELETAL PROTEINS BY NEURONAL DEPOLARIZATION, Cellular and molecular neurobiology, 17(1), 1997, pp. 129-140
Citations number
47
Categorie Soggetti
Neurosciences,"Cell Biology",Biology
ISSN journal
02724340
Volume
17
Issue
1
Year of publication
1997
Pages
129 - 140
Database
ISI
SICI code
0272-4340(1997)17:1<129:MOPONC>2.0.ZU;2-H
Abstract
1, The neuronal cytoskeletal protein tau and the carboxy tails of cyto skeletal proteins neurofilament-M (NF-M) and neurofilament-H (NF-H) ar e phosphorylated on serine residues by the cyclin-dependent kinase cdk -5. 2, In aggregating neuronal-glial cultures we show that veratridine -mediated cation influx causes dephosphorylation of tau, NF-M and NF-H . Dephosphorylation blocked specifically by cyclosporine A but not by okadiac acid at concentrations up to 200 nM. 3. These results suggest that veratridine-triggered cation influx causes activation of PP-2B (c alcineurin) leading to dephosphorylation of these cytoskeletal protein s.