Centralspindlin Centralspindlin is a motor complex implicated in cell division . It contributes to virtually every step in cytokinesis , It is highly conserved in animal cells as a component of the spindle midzone and midbody . Centralspindlin is required for the assembly of the mitotic spindle as well as for microtubule bundling and anchoring of midbody microtubules to the plasma membrane . This complex is also implicated in tethering the spindle apparatus to the plasma membrane during cytokinesis This interaction permits cleavage furrow ingression . In addition, centralspindlin's interaction with the ESCRT III allows for abscission to occur.Structure Centralspindlin is a heteroteramer consisting of two different subunit proteins: A KIF23 dimer A RACGAP1 dimer Both KIF23 and RacGAP1 dimerize via their parallel coiled coil domain. Centralspindlin oligomerizes in order to link the mitotic spindle with the plasma membrane The sequences mediating interactions between KIF23 and RacGAP1 are highly variable between species. However, a high affinity interaction between these subunits is essential for the proper functioning of the Centralspindlin complex.Subunits KIF23 interacts with microtubules at sites of overlap, linking the centraspindlin complex to the mitotic spindle.RacGAP1 recruits ECT2 to the central spindle . ECT2 is a Guanine nucleotide-exchange factor for RhoA . Cytokinesis is initiated when RhoA is activated by ECT2. RacGAP1 is also involved in tethering the central spindle to the plasma membrane. Without this interaction, cytokinesis cannot occur.Interactions A glance at the busy complex Interacts with RhoA and Rac during furrow ingression Recruits cytokinetic effector proteins such as ECT2 Binds microtubule plus-end overlaps characteristic of the central spindle through its KIF23 subunit Recruits the ESCRT III complex in late cytokinesis Promotes cortical accumulation of F-actin and myosin through its RACGAP1 subunit Stabilized through interactions with Aurora B kinase Negatively regulated by 14-3-3 RacGAP1 binds to PRC1 microtubule crosslinker, an interaction that is crucial for maintaining the stability of the spindle midzone.
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