[3] Purification and characterization of myosin II heavy chain kinase A from Dictyostelium

1991 ◽  
pp. 23-34 ◽  
Author(s):  
Quintus G. Medley ◽  
Sheu-Fen Lee ◽  
Graham P. Côté
Keyword(s):  
Heavy Chain ◽  
Myosin Ii ◽  
Purification And Characterization ◽  
Kinase A

Dictyostelium myosin-II heavy-chain kinase A is activated by autophosphorylation: studies with Dictyostelium myosin-II and synthetic peptides

Biochemistry ◽  
1990 ◽  
Vol 29 (38) ◽  
pp. 8992-8997 ◽  
Author(s):  
Quintus G. Medley ◽  
Jean Gariepy ◽  
Graham P. Cote
Keyword(s):  
Heavy Chain ◽  
Synthetic Peptides ◽  
Myosin Ii ◽  
Dictyostelium Myosin ◽  
Kinase A

scholarly journals Structure of the Dictyostelium Myosin-II Heavy Chain Kinase A (MHCK-A) α-kinase domain apoenzyme reveals a novel autoinhibited conformation

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Qilu Ye ◽  
Yidai Yang ◽  
Laura van Staalduinen ◽  
Scott William Crawley ◽  
Linda Liu ◽  
...  
Keyword(s):  
Heavy Chain ◽  
Myosin Ii ◽  
Kinase Domain ◽  
Dictyostelium Myosin ◽  
Kinase A

scholarly journals Myosin heavy-chain kinase A from Dictyostelium possesses a novel actin-binding domain that cross-links actin filaments

2006 ◽  
Vol 395 (2) ◽  
pp. 373-383 ◽  
Author(s):  
Misty Russ ◽  
Daniel Croft ◽  
Omar Ali ◽  
Raquel Martinez ◽  
Paul A. Steimle
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Actin Filaments ◽  
Myosin Ii ◽  
Coiled Coil ◽  
Actin Binding ◽  
Coiled Coil Domain ◽  
Cross Links ◽  
Myosin Heavy Chain Kinase ◽  
Kinase A

Myosin heavy-chain kinase A (MHCK A) catalyses the disassembly of myosin II filaments in Dictyostelium cells via myosin II heavy-chain phosphorylation. MHCK A possesses a ‘coiled-coil’-enriched domain that mediates the oligomerization, cellular localization and actin-binding activities of the kinase. F-actin (filamentous actin) binding by the coiled-coil domain leads to a 40-fold increase in MHCK A activity. In the present study we examined the actin-binding characteristics of the coiled-coil domain as a means of identifying mechanisms by which MHCK A-mediated disassembly of myosin II filaments can be regulated in the cell. Co-sedimentation assays revealed that the coiled-coil domain of MHCK A binds co-operatively to F-actin with an apparent KD of approx. 0.5 μM and a stoichiometry of approx. 5:1 [actin/C(1–498)]. Further analyses indicate that the coiled-coil domain binds along the length of the actin filament and possesses at least two actin-binding regions. Quite surprisingly, we found that the coiled-coil domain cross-links actin filaments into bundles, indicating that MHCK A can affect the cytoskeleton in two important ways: (1) by driving myosin II-filament disassembly via myosin II heavy-chain phosphorylation, and (2) by cross-linking/bundling actin filaments. This discovery, along with other supporting data, suggests a model in which MHCK A-mediated bundling of actin filaments plays a central role in the recruitment and activation of the kinase at specific sites in the cell. Ultimately this provides a means for achieving the robust and highly localized disruption of myosin II filaments that facilitates polarized changes in cell shape during processes such as chemotaxis, cytokinesis and multicellular development.

scholarly journals Isolation, purification, and characterization of fragment B, the NH2-terminal half of the heavy chain of tetanus toxin.

1989 ◽  
Vol 57 (11) ◽  
pp. 3588-3593 ◽  
Author(s):  
M Matsuda ◽  
D L Lei ◽  
N Sugimoto ◽  
K Ozutsumi ◽  
T Okabe
Keyword(s):  
Heavy Chain ◽  
Tetanus Toxin ◽  
Purification And Characterization
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