Phosphorylation of neurofilament proteins by protein kinase C

FEBS Letters

Nixon, Ralph A.²  Jeng, Arco Y.¹  Sihag, Ram K.² 

[1] Research Department, Pharmaceuticals Division, CIBA-Geigy Corporation, Summit, NJ 07901, USA;Ralph Lowell Laboratories, McLean Hospital and Departments of Biological Chemistry and Psychiatry and Program in Neuroscience, Harvard Medical School, Belmont, MA 02178, USA

关键词: Cytoskeletal protein;    Neurofilament protein;    Protein kinase C;    Neuron;    Phosphoprotein;    Peptide mapping;    potein kinase C;    calcium and phosphatidyl-serine-dependent protein kinase;    PMSF;    phenylmethylsulfonyl fluoride;    SDS-PAGE;    SDS-polyacrylamide gel;    TLC;    thin-layer chromatography;    CAMP;    adenosine 3′;    5′-cyclic monophosphate;    DTT;    dithiothreitol;   

DOI  :  10.1016/0014-5793(88)81380-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The low molecular mass (70 kDa) subunit of neurofilaments (NF-L) contains at least three phosphorylation sites in vivo and is phosphorylated by multiple kinases in a site-specific manner [(1987) J. Neurochem. 48, S101; Sihag, R.K. and Nixon, R.A. submitted]. In this study, we observed that the three subunits of neurofilament proteins from retinal ganglion cell neurons are substrates for purified mouse brain protein kinase C. Two-dimensional α-chymotryptic phosphopeptide map analyses of the NF-L subunit demonstrated that protein kinase C phosphorylates four polypeptide sites, two of which incorporate phosphate when retinal ganglion cells are pulse-radiolabeled with [³²P]orthophosphate in vivo.

【 授权许可】

Unknown