Two Nonmuscle Myosin II Heavy Chain Isoforms Expressed in Rabbit Brains:  Filament Forming Properties, the Effects of Phosphorylation by Protein Kinase C and Casein Kinase II, and Location of the Phosphorylation Sites†

Biochemistry ◽  
1998 ◽  
Vol 37 (7) ◽  
pp. 1989-2003 ◽  
Author(s):  
Noriko Murakami ◽  
Ved P. S. Chauhan ◽  
Marshall Elzinga
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Heavy Chain ◽  
Myosin Ii ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Phosphorylation Sites ◽  
Nonmuscle Myosin ◽  
Kinase C ◽  
Nonmuscle Myosin Ii

Inhibition of protein kinase C- and casein kinase II-mediated phosphorylation of GAP-43 by S100β

1994 ◽  
Vol 25 (3-4) ◽  
pp. 297-304 ◽  
Author(s):  
Li-Hsien Lin ◽  
Linda J. Van Eldik ◽  
Neil Osheroff ◽  
Jeanette J. Norden
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Kinase C

scholarly journals Conservedin VivoPhosphorylation of Calnexin at Casein Kinase II Sites as Well as a Protein Kinase C/Proline-directed Kinase Site

1998 ◽  
Vol 273 (27) ◽  
pp. 17227-17235 ◽  
Author(s):  
Hetty N. Wong ◽  
Malcolm A. Ward ◽  
Alexander W. Bell ◽  
Eric Chevet ◽  
Satty Bains ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Kinase C

scholarly journals Metastasis-associated Mts1 (S100A4) Protein Modulates Protein Kinase C Phosphorylation of the Heavy Chain of Nonmuscle Myosin

1998 ◽  
Vol 273 (16) ◽  
pp. 9852-9856 ◽  
Author(s):  
Marina Kriajevska ◽  
Svetlana Tarabykina ◽  
Igor Bronstein ◽  
Norman Maitland ◽  
Mikhail Lomonosov ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Heavy Chain ◽  
Nonmuscle Myosin ◽  
S100a4 Protein ◽  
Kinase C

scholarly journals Phosphorylation of Canine Distemper Virus P Protein by Protein Kinase C-ζ and Casein Kinase II

Virology ◽  
1997 ◽  
Vol 232 (1) ◽  
pp. 198-206 ◽  
Author(s):  
Zheng Liu ◽  
Clayton C. Huntley ◽  
Bishnu P. De ◽  
Tapas Das ◽  
Amiya K. Banerjee ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Canine Distemper Virus ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Canine Distemper ◽  
Kinase C ◽  
P Protein

scholarly journals Purification and characterization of echinoderm casein kinase II. Regulation by protein kinase C

1992 ◽  
Vol 283 (3) ◽  
pp. 829-837 ◽  
Author(s):  
J S Sanghera ◽  
L A Charlton ◽  
H B Paddon ◽  
S L Pelech
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Beta Subunit ◽  
Alpha Subunit ◽  
Sea Star ◽  
Sequential Fractionation ◽  
Germinal Vesicle Breakdown ◽  
Kinase C

Casein kinase II (CKII) is one of several protein kinases that become activated before germinal-vesicle breakdown in maturing sea-star oocytes. Echinoderm CKII was purified over 11,000-fold with a recovery of approximately 10% by sequential fractionation of the oocyte cytosol on tyrosine-agarose, heparin-agarose, casein-agarose and MonoQ. The purified enzyme contained 45, 38 and 28 kDa polypeptides, which corresponded to its alpha, alpha' and beta subunits respectively. The beta-subunit was autophosphorylated on one major tryptic peptide on serine residues, whereas the alpha'-subunit incorporated phosphate into at least two tryptic peptides primarily on threonine residues. Western-blotting analysis of sea-star oocyte extracts with two different anti-peptide antibodies that recognized conserved regions of the alpha-subunit indicated that the protein levels of the alpha- and alpha'-subunits of CKII were unchanged during oocyte maturation. The purified CKII was partly inactivated (by 25%) by preincubation with protein-serine/threonine phosphatase 2A, but protein-tyrosine phosphatases had no effect. The beta-subunit of CKII was phosphorylated on a serine residue(s) up to 0.54 mol of P/mol of beta-subunit by purified protein kinase C, and this correlated with a 1.5-fold enhancement of its phosphotransferase activity with phosvitin as a substrate. CKII was not a substrate for the maturation-activated myelin basic protein kinase p44mpk from sea-star oocytes, nor for cyclic-AMP-dependent protein kinase. These studies point to possible regulation of CKII by protein phosphorylation.

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