scholarly journals Cell type-specific upregulation of myristoylated alanine-rich C kinase substrate and protein kinase C-α, -β I, -β II, and -δ in microglia following kainic acid-induced seizures

2006 ◽  
Vol 38 (3) ◽  
pp. 310-319 ◽  
Author(s):  
Su-Yong Eun ◽  
Eun Hae Kim ◽  
Kee-Seok Kang ◽  
Hwa Jung Kim ◽  
Sangmee Ahn Jo ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Kainic Acid ◽  
Cell Type ◽  
Kinase Substrate ◽  
Kinase C ◽  
Cell Type Specific

scholarly journals Gene- and cell-type-specific effects of signal transduction cascades on metal-regulated gene transcription appear to be independent of changes in the phosphorylation of metal-response-element-binding transcription factor-1

2004 ◽  
Vol 382 (1) ◽  
pp. 33-41 ◽  
Author(s):  
Huimin JIANG ◽  
Kai FU ◽  
Glen K. ANDREWS
Keyword(s):  
Transcription Factor ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinases ◽  
Cell Type ◽  
Specific Effects ◽  
Kinase C ◽  
Cell Type Specific ◽  
Transcription Factor 1

Post-translational modification of MTF-1 (metal-response-element-binding transcription factor-1) was suggested to play a role in its metalloregulatory functions. In the present study, pulse labelling and two-dimensional electrophoresis–Western blotting were used to demonstrate that, although MTF-1 is highly modified in vivo, its phosphorylation level does not rapidly change in response to metals, nor does its overall modification pattern. Recombinant MTF-1 was found to serve as an in vitro substrate for casein kinase II, c-Jun N-terminal kinase and protein kinase C, but inhibition of these kinases in vivo did not significantly change the modification pattern of MTF-1. Northern blotting revealed that inhibitors of casein kinase II and c-Jun N-terminal kinase severely attenuate the metal-induced transcription of the native chromatin-packaged metallothionein-I and zinc transporter-1 genes, whereas protein kinase C inhibitors exerted gene- and cell-type-specific effects on the metal regulation and basal expression of these two genes. A chromatin immunoprecipitation assay was used to demonstrate that none of these inhibitors prevent the metal-dependent recruitment of MTF-1 to the MT-I promoter. In brief, results of the present study suggest that protein kinases may not alter the phosphorylation state of MTF-1 during the rapid-response phase to metals, nor do they regulate the metal-dependent formation of a stable MTF-1–chromatin complex. Instead, protein kinases may exert their interdependent effects on metal-induced gene expression by acting on cofactors that interact with MTF-1.

scholarly journals Cell type-specific expression of protein kinase C isozymes in the rabbit cerebellum.

1988 ◽  
Vol 263 (10) ◽  
pp. 4523-4526 ◽  
Author(s):  
H Hidaka ◽  
T Tanaka ◽  
K Onoda ◽  
M Hagiwara ◽  
M Watanabe ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Type ◽  
Specific Expression ◽  
Kinase C ◽  
Cell Type Specific Expression ◽  
Cell Type Specific

scholarly journals Phosphorylation of the myristoylated protein kinase C substrate MARCKS by the cyclin E–cyclin-dependent kinase 2 complex in vitro

1999 ◽  
Vol 340 (3) ◽  
pp. 775-782 ◽  
Author(s):  
Stéphane MANENTI ◽  
Emiko YAMAUCHI ◽  
Odile SOROKINE ◽  
Martine KNIBIEHLER ◽  
Alain VAN DORSSELAER ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cyclin E ◽  
Cyclin Dependent Kinase ◽  
Kinase Substrate ◽  
Cyclin Dependent Kinases ◽  
Kinase C ◽  
Cdk2 Complex

The myristoylated alanine-rich C-kinase substrate (MARCKS) purified from brain was recently characterized as a proline-directed kinase(s) substrate in vivo [Taniguchi, Manenti, Suzuki and Titani (1994) J. Biol. Chem. 269, 18299-18302]. Here we have investigated the phosphorylation of MARCKS by various cyclin-dependent kinases (Cdks) in vitro. We established that Cdk2, Cdk4 and, to a smaller extent, Cdk1 that have been immunoprecipitated from cellular extracts phosphorylate MARCKS. Comparison of MARCKS phosphorylation by protein kinase C (PKC) and by the purified cyclin E-Cdk2 complex suggested that two residues were phosphorylated by Cdk2 under these conditions. To identify these sites, Cdk2-phosphorylated MARCKS was digested with lysyl endoprotease and analysed by electrospray MS. Comparison with the digests obtained from the unphosphorylated protein demonstrated that two peptides, Gly12-Lys30 and Ala138-Lys152, were phosphorylated by cyclin E-Cdk2. The identity of these peptides was confirmed by automatic Edman degradation. On the basis of the consensus phosphorylation sequence described for Cdk2, and on MS/MS analysis of the Ala138-Lys152 peptide, we concluded that Ser27, one of the phosphorylation sites identified in vivo, and Thr150 were the Cdk2 targets in vitro. None of the other sites described in vivo were phosphorylated in these conditions. Interestingly, a preliminary phosphorylation of MARCKS by PKC improved the initial rate of phosphorylation by Cdk2 without modifying the number of sites concerned. In contrast, phosphorylation of MARCKS by Cdk2 did not significantly affect further phosphorylation by PKC.

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