EC Number   |
General Information |
Reference |
|---|
   5.6.1.4 | evolution |
enzyme KifC3 is a C-terminal kinesin of the kinesin-14 family |
733397 |
| 5.6.1.4 | evolution |
kinesin-14 represents a subfamily of kinesins that are nonprocessive, promote microtubule (MT)2 minus-end-directed force generation, and contain C-terminal motor domains that are dimerized through an N-terminal coiled coil. Kinesin-14s use an microtubule minus-end-directed rotation or bending of the coiled-coil stalk to generate force |
734196 |
| 5.6.1.4 | evolution |
Ncd is a member of kinesin superfamily, kinesin-14 subfamily motors that uses the power stroke, a lever-like pivoting action of a long and stiff element, to exert force and generate movement |
719508 |
| 5.6.1.4 | malfunction |
knockdown of KifC3 using RNAi results in an increase of cells with perinuclear-clustered peroxisomes, indicating enhanced minus-end directed motility of peroxisomes leading to peroxisomal clustering at the microtubule-organizing center. The peroxisomal phenotype is cell cycle phase independent, while microtubules are essential for phenotype formation |
733397 |
| 5.6.1.4 | metabolism |
compared to dynein, representing a minus-motor and therefore transporting cargoes to the cell center, the kinesin's direction of transport is dependent on the position of their motor domain. C-kinesins are typically minus-motors. Transport of peroxisomes along microtubules in mammalian cells occurs by the motor proteins cytoplasmic dynein and kinesin-1 The enzyme KifC3 knockdown also affects the morphology of mitochondria and endoplasmic reticulum, phenotype |
733397 |
| 5.6.1.4 | metabolism |
key differences in the ATPase cycles of Kar3Vik1 and Kar3Cik1, these two motors have distinctive biological functions |
734196 |
| 5.6.1.4 | more |
Kar3, a microtubule minus-end-directed kinesin-14, dimerizes with either Vik1 or Cik1. The C-terminal globular domain of Vik1 exhibits the structure of a kinesin motor domain and binds microtubules independently of Kar3 but lacks a nucleotide binding site. The tight binding of Kar3 to the microtubule destabilizes the Vik1 interaction with the microtubule, positioning Kar3Vik1 for the start of the powerstroke. Rapid ATP binding to Kar3 is associated with rotation of the coiled-coil stalk, and the post-powerstroke ATP hydrolysis at 26/s is independent of Vik1, providing further evidence that Vik1 rotates with the coiled coil during the powerstroke. Detachment of Kar3Vik1 from the microtubule completes the cycle and allows the motor to return to its initial conformation |
734196 |
| 5.6.1.4 | more |
the C-terminal segment of the kinesin-14 subfamily is formed by residues that extend beyond the a6 helix |
719508 |
| 5.6.1.4 | physiological function |
can form microtubule asters without additional factors |
720088 |
| 5.6.1.4 | physiological function |
Kar3 is a kinesin motor that facilitates chromosome segregation during cell division |
713213 |
