of microtubule filaments, and assembly of central-spindle-mediating proteins, including but not limited to Kinesin-4. PRC1 dimers, required for the high-affinity interaction with Kinesin-4, recruit Kinesin-4 to regions of antiparallel microtubule overlap, where Kinesin-4, a plus-end directed motor protein that inhibits microtubule dynamics, helps to form length-dependent end tags that help stabilize and regulate spindle microtubule assembly within cytokinesis. This PRC1-Kinesin-4 complex differentially identifies and regulates the spindle midzone microtubules during cell division. This regulation is crucial in order for cytokinesis to progress properly. Interactions PRC1 is a non-motor microtubule-associated protein (MAP) whose C-terminal spectrin domain (aa 341-640) binds microtubules with micromolar affinity (0.6 +/- 0.3uM) PRC1 has been shown to interact with TRIM37. PRC1 interacts with Kinesin-4 that plays an important role in crossing spindle microtubules and setting midzone length in mammalian cytokinesis. PRC1 is negatively modulated by CDKs, particularly CDK1. PLK1 negatively regulates PRC1 through phosphorylation at Thr-602, near the C-terminus of PRC1, only after dephosphorylation of PRC1 at an inhibitory CDK1 site. PRC1 binds directly to CYK-4 subunit of the centralspindlin complex to stabilise the central spindle. References Further reading External links