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Literature summary for 2.7.11.7 extracted from

  • Underwood, J.; Greene, J.; Steimle, P.A.
    Identification of a new mechanism for targeting myosin II heavy chain phosphorylation by Dictyostelium myosin heavy chain kinase B (2010), BMC Res. Notes, 3, 56.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of FLAG-tagged full-length MHCK-B in Dictyostelium cells, in AX2, mhkB-null, and mhkA/B/C-null cell lines. Expression of GST-tagged wild-type full-length and MHCKB truncation mutants Dictyostelium discoideum

Protein Variants

Protein Variants Comment Organism
additional information generation of the MHCKB truncation lacking only the WD-repeat domain and of a mutant lacking the N-rich region. Cells overexpressing the MHCK mutant lacking only the WD-repeat domain exhibit cytokinesis defects and decreased myosin II assembly Dictyostelium discoideum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Dictyostelium discoideum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [myosin heavy-chain] Dictyostelium discoideum
-
ADP + [myosin heavy-chain] phosphate
-
?

Organism

Organism UniProt Comment Textmining
Dictyostelium discoideum P90648
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein 15 to 20 autophosphorylation sites in MHCK-B reside in the N-rich region of the kinase. Autophosphorylation of full-length MHCK-B has no effect on the kinase activity of the enzyme Dictyostelium discoideum

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged wild-type full-length and MHCKB truncation mutants by glutathione affinity chromatography Dictyostelium discoideum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + MH1 peptide
-
Dictyostelium discoideum ADP + MH1 peeptide phosphate
-
?
ATP + [myosin heavy-chain]
-
Dictyostelium discoideum ADP + [myosin heavy-chain] phosphate
-
?

Synonyms

Synonyms Comment Organism
MHCK-B
-
Dictyostelium discoideum
myosin heavy chain kinase B
-
Dictyostelium discoideum
myosin II heavy chain kinase B
-
Dictyostelium discoideum

Cofactor

Cofactor Comment Organism Structure
ATP
-
Dictyostelium discoideum

General Information

General Information Comment Organism
malfunction removal of the N-rich region severely compromises MHC phosphorylation by the catalytic domain. Removal of both the N-rich and WD-repeat domains renders the catalytic domain barely able to phosphorylate MHC above detectable levels, whereas the truncation containing the N-rich region can still use MHC as a substrate, albeit at about 30% of that displayed by the full-length kinase. But the innate kinase activity of the catalytic domain is not lost upon removal of the N-rich region and/or the WD-repeat domain of MHCK-B since all three versions of MHCK-B phosphorylated MH-1 peptide to the same level Dictyostelium discoideum
additional information mechanism for targeting myosin II heavy chain phosphorylation by myosin heavy chain kinase B, overview. An intrinsically unstructured, and asparagine-rich, region of a MHCK-B can mediate specific targeting of the kinase to phosphorylate myosin II heavy chain involving a direct binding interaction with myosin II filaments, while the the WD repeat domain is not absolutely required in MHCK-B substrate targeting, in contrast to isozyme MHCK-A. The N-rich region facilitates phosphorylation of MHC by binding directly to myosin II filaments Dictyostelium discoideum
physiological function heavy chain phosphorylation plays a central role in regulating myosin II bipolar filament assembly in Dictyostelium Dictyostelium discoideum