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Literature summary for 5.6.1.2 extracted from

  • Huang, J.; Roberts, A.J.; Leschziner, A.E.; Reck-Peterson, S.L.
    Lis1 acts as a clutch between the ATPase and microtubule-binding domains of the dynein motor (2012), Cell, 150, 975-986.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.6.1.2

Activating Compound

Activating Compound Comment Organism Structure
additional information microtubule-stimulated ATPase activity of GST-dynein331 kDa in the presence of Lis1 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information in the presence of microtubules, the maximal ATPase rate of constructed GST-dynein331 kDa/Lis1 retains about 90% of the value for GST-dynein331 kDa alone Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
lissencephaly protein Lis1 the lissencephaly protein Lis1 regulates the mechanical behavior of cytoplasmic dynein, the primary minus-end-directed microtubule motor, regulatory mechanism. Rather than binding to the main ATPase site within dynein's AAA+ ring or its microtubule-binding stalk directly, dimeric Lis1 engages the interface between these elements. Lis1 causes individual dynein motors to remain attached to microtubules for extended periods, even during cycles of ATP hydrolysis that canonically induces detachment. Lis1 operates like a clutch that prevents dynein's ATPase domain from transmitting a detachment signal to its track-binding domain. The Lis1 beta propeller domain contains regulatory elements that act on dynein's motor and Lis1 alters allosteric communication between dynein's ATPase and microtubule-binding domains Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + a dynein associated with a microtubule at position n Saccharomyces cerevisiae
-
 ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + a dynein associated with a microtubule at position n
-
 Saccharomyces cerevisiae ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end)
-
 ?

Synonyms

Synonyms Comment Organism
dynein's ATPase
-
 Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution the dynein ATpase belongs to the AAA+ ATPases Saccharomyces cerevisiae
additional information dynein's architectural features make interdomain communication a central part of its mechanism and an additional potential target for regulation, overview Saccharomyces cerevisiae
physiological function conserved mechanism for dynein functions in living cells that require prolonged microtubule attachments. The lissencephaly protein Lis1 regulates the mechanical behavior of cytoplasmic dynein, the primary minus-end-directed microtubule motor, regulatory mechanism. Rather than binding to the main ATPase site within dynein's AAA+ ring or its microtubule-binding stalk directly, dimeric Lis1 engages the interface between these elements. Lis1 causes individual dynein motors to remain attached to microtubules for extended periods, even during cycles of ATP hydrolysis that canonically induces detachment. Lis1 operates like a clutch that prevents dynein's ATPase domain from transmitting a detachment signal to its track-binding domain. The Lis1 beta propeller domain contains regulatory elements that act on dynein's motor and Lis1 alters allosteric communication between dynein's ATPase and microtubule-binding domains Saccharomyces cerevisiae