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Phosphorylation of neurofilament proteins by protein kinase C
Author(s) -
Sihag Ram K.,
Jeng Arco Y.,
Nixon Ralph A.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81380-2
Subject(s) - neurofilament , phosphorylation , protein subunit , kinase , phosphopeptide , microbiology and biotechnology , protein kinase a , cyclin dependent kinase 5 , chemistry , biochemistry , retinal ganglion cell , biology , mitogen activated protein kinase kinase , retinal , immunohistochemistry , gene , immunology
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 [ 32 P]orthophosphate in vivo.