EC Number   |
General Information |
Reference |
|---|
   5.6.1.2 | evolution |
dyneins are members of the AAA+ superfamily of ring-shaped enzymes |
735286 |
| 5.6.1.2 | evolution |
the dynein ATpase belongs to the AAA+ ATPases |
733640 |
| 5.6.1.2 | more |
dynein ATPases are the largest known cytoskeletal motors and perform critical functions in cells: carrying cargo along microtubules in the cytoplasm and powering flagellar beating. ATP-driven remodeling of the linker domain in the dynein motor, structure-function analysis of the cytoplasmic dynein motor domain, motor mechanism, overview. Driving sliding between microtubules with energy that is supplied by interactions with the AAA+ modules. Conserved architecture of the head domains of cytoplasmic dynein, an open nucleotide-binding pocket at AAA1 is an intrinsic feature of dynein structure in the absence of nucleotide. Modeling |
735286 |
| 5.6.1.2 | more |
dynein ATPases are the largest known cytoskeletal motors and perform critical functions in cells: carrying cargo along microtubules in the cytoplasm and powering flagellar beating. ATP-driven remodeling of the linker domain in the dynein motor, structure-function analysis of the flagellar dynein-c, motor mechanism, overview. Driving sliding between microtubules with energy that is supplied by interactions with the AAA+ modules. Architecture of the head domains of axonemal dynein-c comprising an asymmetric ring-like structure with the linker domain arching over one face. Modeling |
735286 |
| 5.6.1.2 | more |
dynein's architectural features make interdomain communication a central part of its mechanism and an additional potential target for regulation, overview |
733640 |
| 5.6.1.2 | more |
potential mechanisms of the reversible temperature-dependent immobilization of fowl sperm |
-, 735303 |
| 5.6.1.2 | physiological function |
a two-headed inner dynein arm for regulation of flagellar blending |
712983 |
| 5.6.1.2 | 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 |
733640 |
| 5.6.1.2 | physiological function |
cytoplasmic dynein is an AAA+ motor responsible for intracellular cargo transport and force generation along microtubules |
-, 751690 |
| 5.6.1.2 | physiological function |
dynein acts as a motor protein and converts the energy stored in ATP into movement by coupling the cycle of ATP hydrolysis to structural changes in the motor protein. The dynein motor family is composed of several axonemal forms that drive the beating of cilia, flagella and two cytoplasmic forms that are responsible for a range of cellular functions such as cargo transport, mitosis, and cell polarization |
711714 |
