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MCAK is involved in directional migration and invasion of tumor cells.
the Aurora B (show AURKB Proteins)-PLK1 signaling at the kinetochore orchestrates MCAK activity, which is essential for timely correction of aberrant kinetochore attachment to ensure accurate chromosome segregation during mitosis.
MCAK activity is modulated by Plk1 phosphorylation on S632/S633 in mitosis.
These results demonstrate that the structural change of Kif2C-ATP upon binding to microtubule ends is sufficient for tubulin (show TUBB Proteins) release, whereas ATP hydrolysis is not required
Ras regulates KIF2C to control cell migration pathways in transformed human bronchial epithelial cells.
A dynamic interaction of MCAK-TIP150 (show KIAA0774 Proteins) orchestrated by Aurora A (show AURKA Proteins)-mediated phosphorylation governs entosis via regulating microtubule plus-end dynamics and cell rigidity.
this study suggests a new mechanism by which Plk1 regulates MCAK: by regulating its degradation and hence controlling its turnover in mitosis.
up-regulation of KIF2C and KIF2A by ERK1/2 caused aberrant lysosomal positioning and mTORC1 activity in a mutant K-Ras-dependent cancer and cancer model.
A Rac1-Aurora A (show AURKA Proteins)-MCAK signaling pathway mediates endothelial cell polarization and directional migration by promoting regional differences in microtubule dynamics.
result suggested E403K mutation in mitotic centromere-associated kinesin protein (show KIF2B Proteins) as highly damaging and showed strong concordance to the previously observed colorectal cancer mutations aggregation tendency and energy value changes
PAK1 (show PAK1 Proteins) phosphorylates MCAK and regulates both its localization and function.
MCAK appears to possess a unique distribution and function in oocyte maturation.
MCAK contributes to chromosome alignment in meiosis I, but is not necessary for preventing chromosome segregation errors.
Possible functions of MCAK at the inner centromere domain and at the perikinetochoric ring during both meiotic divisions.
Shugoshin 2 is necessary for the loading of MCAK at the inner centromere, but is dispensable for the loading of the outer kinetochore proteins BubR1 (show BUB1B Proteins) and CENP-E (show CENPE Proteins).
MCAK colocalized with NuMA and XMAP215 at the center of Ran asters where its activity is regulated by Aurora A (show AURKA Proteins)-dependent phosphorylation of S196, which contributes to proper pole focusing
This study reveals a new role for Aurora B (show AURKB Proteins), which is to prevent excess MCAK binding to chromatin to facilitate chromatin-nucleated spindle assembly.
MCAK regulation of cytoplasmic and spindle-associated (show HAUS1 Proteins) microtubules can be differentiated by Aurora B (show AURKB Proteins)-dependent phosphorylation
These data support a model in which Nup98 (show NUP98 Proteins) interacts with microtubules and antagonizes MCAK activity, thus promoting bipolar spindle assembly.
The protein encoded by this gene is a member of kinesin-like protein family. Proteins of this family are microtubule-dependent molecular motors that transport organelles within cells and move chromosomes during cell division. This protein is important for anaphase chromosome segregation and may be required to coordinate the onset of sister centromere separation.
kinesin family member 2C
, kinesin-like protein KIF2C
, kinesin-like protein KIF2C-like
, kinesin-like 6
, kinesin-like protein 6
, mitotic centromere-associated kinesin
, kinesin-related protein 2
, Kinesin-like protein 6
, kinesin central motor 1