Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | microtubule-stimulated ATPase activity of GST-dynein331 kDa in the presence of Lis1 | Saccharomyces cerevisiae |
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 | 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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Saccharomyces cerevisiae |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
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 | Comment | Organism |
---|---|---|
dynein's ATPase | - |
Saccharomyces cerevisiae |
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 |