Protein kinase C phosphorylates both the light chains and the head portion of the heavy chains of brain myosin
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference28 articles.
1. Myosin Structure and Function in Cell Motility
2. Myosins of Nonmuscle Cells
3. Phosphorylation of myosin in smooth muscle and non-muscle cells. In vitro and in vivo effects
4. Phosphorylation of smooth muscle heavy meromyosin by calcium-activated, phospholipid-dependent protein kinase. The effect on actin-activated MgATPase activity.
5. Protein kinase C modulates in vitro phosphorylation of the smooth muscle heavy meromyosin by myosin light chain kinase.
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1. Estrogen Modulation of MgATPase Activity of Nonmuscle Myosin-II-B Filaments;Endocrinology;2007-01-01
2. Lysophosphatidic acid stimulates actomyosin contraction in astrocytes;Journal of Neuroscience Research;1998-08-01
3. 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;1998-01-30
4. Phospholipid binding, phosphorylation by protein kinase C, and filament assembly of the COOH terminal heavy chain fragments of nonmuscle myosin II isoforms MIIA and MIIB;Biochemistry;1995-12
5. Direct binding of myosin II to phospholipid vesicles via tail regions and phosphorylation of the heavy chains by protein kinase C.;Journal of Biological Chemistry;1994-06
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