Identification of the serine residue phosphorylated by protein kinase C in vertebrate nonmuscle myosin heavy chains.
作者： Mary Anne Conti , James R. Sellers , Robert S. Adelstein , Marshall Elzinga
DOI: 10.1021/BI00218A012
关键词: Biology 、 Peptide 、 Biochemistry 、 Protein kinase C 、 Serine 、 Amino acid 、 Residue (chemistry) 、 Myosin 、 Peptide sequence 、 Myosin light-chain kinase 、 Molecular biology
摘要: Two-dimensional mapping of the tryptic phosphopeptides generated following in vitro protein kinase C phosphorylation myosin heavy chain isolated from human platelets and chicken intestinal epithelial cells shows a single radioactive peptide. These peptides were found to comigrate, suggesting that they identical, amino acid sequence analysis platelet peptide yielded -Glu-Val-Ser-Ser(PO4)-Leu-Lys-. Inspection for cell (196 kDa) derived cDNA cloning showed this was identical with present near carboxyl terminal predicted alpha-helix rod. Although other vertebrate nonmuscle chains retain neighboring sequences as well serine residue phosphorylated by C, is notably absent all smooth muscle (both 204 200 sequenced date.
acs.org
sci-hub.se 参考文章(34)
K E Kamm, L C Hsu, Y Kubota, J T Stull, Phosphorylation of smooth muscle myosin heavy and light chains. Effects of phorbol dibutyrate and agonists. Journal of Biological Chemistry. ,vol. 264, pp. 21223- 21229 ,(1989) , 10.1016/S0021-9258(19)30070-5
M Ikebe, D J Hartshorne, M Elzinga, Phosphorylation of the 20,000-dalton light chain of smooth muscle myosin by the calcium-activated, phospholipid-dependent protein kinase. Phosphorylation sites and effects of phosphorylation. Journal of Biological Chemistry. ,vol. 262, pp. 9569- 9573 ,(1987) , 10.1016/S0021-9258(18)47971-9
S Umemoto, A R Bengur, J R Sellers, Effect of multiple phosphorylations of smooth muscle and cytoplasmic myosins on movement in an in vitro motility assay Journal of Biological Chemistry. ,vol. 264, pp. 1431- 1436 ,(1989) , 10.1016/S0021-9258(18)94205-5
H A Singer, J W Oren, H A Benscoter, Myosin light chain phosphorylation in 32P-labeled rabbit aorta stimulated by phorbol 12,13-dibutyrate and phenylephrine. Journal of Biological Chemistry. ,vol. 264, pp. 21215- 21222 ,(1989) , 10.1016/S0021-9258(19)30069-9
S Kawamoto, R S Adelstein, The heavy chain of smooth muscle myosin is phosphorylated in aorta cells. Journal of Biological Chemistry. ,vol. 263, pp. 1099- 1102 ,(1988) , 10.1016/S0021-9258(19)57269-6
S Kawamoto, A R Bengur, J R Sellers, R S Adelstein, In situ phosphorylation of human platelet myosin heavy and light chains by protein kinase C. Journal of Biological Chemistry. ,vol. 264, pp. 2258- 2265 ,(1989) , 10.1016/S0021-9258(18)94170-0
M Nishikawa, J R Sellers, R S Adelstein, H Hidaka, Protein kinase C modulates in vitro phosphorylation of the smooth muscle heavy meromyosin by myosin light chain kinase. Journal of Biological Chemistry. ,vol. 259, pp. 8808- 8814 ,(1984) , 10.1016/S0021-9258(17)47225-5
N Murakami, G Healy-Louie, M Elzinga, Amino acid sequence around the serine phosphorylated by casein kinase II in brain myosin heavy chain. Journal of Biological Chemistry. ,vol. 265, pp. 1041- 1047 ,(1990) , 10.1016/S0021-9258(19)40156-7
C House, R E Wettenhall, B E Kemp, The influence of basic residues on the substrate specificity of protein kinase C. Journal of Biological Chemistry. ,vol. 262, pp. 772- 777 ,(1987) , 10.1016/S0021-9258(19)75853-0
R I Ludowyke, I Peleg, M A Beaven, R S Adelstein, Antigen-induced secretion of histamine and the phosphorylation of myosin by protein kinase C in rat basophilic leukemia cells. Journal of Biological Chemistry. ,vol. 264, pp. 12492- 12501 ,(1989) , 10.1016/S0021-9258(18)63885-2