Myosin heavy chain kinase

Gallus gallus (two myosin heavy-chain kinases a Ca /calmodulin dependent and a Ca /calmodulin independent enzyme [10,11] the Ca /cal-modulin dependent heavy chain kinase has several properties in common with the family of type II calmodulin-dependent protein kinases [11]) [10,... 

Dictyostelium discoideum (myosin II heavy chain kinase MHCK A [26] gene MHKA or MHCKA, myosin heavy chain kinase A [13]) [13, 26]... 

Dictyostelium discoideum (gene MHCK, myosin heavy chain kinase [13])... 

S ATP -I- myosin I heavy chain <1, 2, 9-11> (<10> major site of phosphorylation is Ser8 [22] <2> 35 kDa trypsin fragment of the C-terminus of the maximally activated, phosphorylated enzyme is fully catalytically active and contains 2 thirds of the autophosphorylation sites of the native enzyme [20] <9,10> substrate myosin ID [19,22] <2> higher activity with membrane-bound substrate myosin I [17] <2> substrates are heavy chains of myosin lA and IB [6,7,17] <2,11> substrate is heavy chain of myosin IC [7,23,24] <2> a basic amino acid is essential on amino-terminal side of phosphorylation site, two are preferable, and a Tyr-residue is essential two residues away on the COOH-terminal side [7] <2> contains two myosin heavy chain kinases one for myosin I and one for myosin II... 

Cote, G.P. Bukiejko, U. Purification and characterization of a myosin heavy chain kinase from Dictyostelium discoideum. J. Biol. Chem., 262, 1065-1072 (1987)... 

Rieker, J.P. Swanljung-Collins, H. Montibeller, J. Collins, J.H. Isolation and characterization of calmodulin-dependent myosin heavy chain kinase from intestinal brush border. Methods EnzymoL, 139, 105-114 (1987)... 

Murakami, N. Matsumura, S. Kumon, A. Purification and identification of myosin heavy chain kinase from bovine brain. J. Biochem., 95, 651-660 (1984)... 

Nagasaki, A. Itoh, G. Yumura, S. Uyeda, T.Q. Novel myosin heavy chain kinase involved in disassembly of myosin II filaments and efficient cleavage in mitotic dictyostelium cells. Mol. Biol. Cell, 13, 4333-4342 (2002)... 

Rico, M. Egelhoff, T.T. Myosin heavy chain kinase B participates in the regulation of myosin assembly into the cytoskeleton. J. Cell. Biochem., 88, 521-532 (2003)... 

Ravid, S. Spudich, J.A. Membrane-bound Dictyostelium myosin heavy chain kinase a developmentally regulated substrate-specific member of the protein kinase C family. Proc. Natl. Acad. Sci. USA, 89, 5877-5881 (1992)... 

Kolman, M.F. Futey, L.M. Egelhoff, T.T. Dictyostelium myosin heavy chain kinase A regulates myosin localization during growth and development. J. Cell. Biol., 132, 101-109 (1996)... 

Steimle, P.A. Licate, L. Cote, G.P. Egelhoff, T.T. Lamellipodial localization of Dictyostelium myosin heavy chain kinase A is mediated via F-actin binding by the coiled-coil domain. FEBS Lett., 516, 58-62 (2002)... 

Stcimle PA, Naismith T, Licate L et al. WD repeat domains target Dictyostclium myosin heavy chain kinases by binding directly to myosin filaments. J Biol Chem 2001 276(9) 6853-60. 

Contraction in amoeboid cells makes use of nonmuscle forms of myosin type II whieh form bipolar thiek filaments in the cytoplasm and in association with the actin filaments [23, 54]. In Dictyostelium, actin filaments form a eortieal shell directly under the plasma membrane, with random orientation of the filaments [132]. Activation of myosin contractile activity by phosphorylation of the myosin light ehain protein results in contraction of the cortical network [54, 110], It is unclear whether this contraetion is uniform throughout the eell or whether there is spatial regulation of the activity. In polarized motile Dictyostelium cells, myosin is concentrated at the rear of the cell [31], which could maintain the polarization, while a myosin heavy chain kinase (which phosphorylates the myosin heavy chain protein and inhibits thick filament formation), is localized at the front of the cell. 

Steimle, P.A., Yumura, S., Cote, G.P et d. (2001). Recruitment of a myosin heavy chain kinase to actin-rich protrusions in Dictyostelium. Curr. Biol. 11, 708—713. 

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