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Literature summary for 5.6.1.8 extracted from

  • Mizui, T.; Sekino, Y.; Yamazaki, H.; Ishizuka, Y.; Takahashi, H.; Kojima, N.; Kojima, M.; Shirao, T.
    Myosin II ATPase activity mediates the long-term potentiation-induced exodus of stable F-actin bound by drebrin A from dendritic spines (2014), PLoS ONE, 9, e85367.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.8

Activating Compound

Activating Compound Comment Organism Structure
additional information myosin II seems to be activated by a rapid actin-linked mechanism rather than slow myosin light chain phosphorylation Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
(S)-(2)-blebbistatin
-
 Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + myosin bound to actin filament at position n Rattus norvegicus
-
 ADP + phosphate + myosin bound to actin filament at position n+1
-
 ?
ATP + H2O + myosin bound to actin filament at position n Rattus norvegicus Wistar
-
 ADP + phosphate + myosin bound to actin filament at position n+1
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-
Rattus norvegicus Wistar
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
hippocampal cell line
-
 Rattus norvegicus
-
neuron
-
 Rattus norvegicus
-
spinal column
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + myosin bound to actin filament at position n
-
 Rattus norvegicus ADP + phosphate + myosin bound to actin filament at position n+1
-
 ?
ATP + H2O + myosin bound to actin filament at position n
-
 Rattus norvegicus Wistar ADP + phosphate + myosin bound to actin filament at position n+1
-
 ?

Synonyms

Synonyms Comment Organism
myosin II ATPase
-
 Rattus norvegicus

General Information

General Information Comment Organism
physiological function in drebrin A (DA-actin) from dendritic spines, DA-actin exodus is blocked by myosin II ATPase inhibitor, but is not blocked by myosin light chain kinase or Rho-associated kinase inhibitors, indicating that myosin II mediates the interaction between NMDA receptor activation and DA-actin exodus in long-term potentiation induction. Glutamate-induced DA-actin exodus is also dependent on myosin II ATPase activity. Myosin II seems to be activated by a rapid actin-linked mechanism rather than slow myosin light chain phosphorylation. The myosin-II mediated DA-actin exodus might be an initial event in LTP induction, triggering actin polymerization and spine enlargement Rattus norvegicus