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Protein regulator of cytokinesis 1

Domain

Microtubule binding occurs via a basic patch in the central spectrin-like domain and requires also the unstructured C-terminal domain.

Function

Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression (PubMed:17409436).

Post-translational modifications

Phosphorylation by CDK1 in early mitosis holds PRC1 in an inactive monomeric state, during the metaphase to anaphase transition, PRC1 is dephosphorylated, promoting interaction with KIF4A, which then translocates PRC1 along mitotic spindles to the plus ends of antiparallel interdigitating microtubules. Dephosphorylation also promotes MT-bundling activity by allowing dimerization. Phosphorylation by CDK1 prevents PLK1-binding: upon degradation of CDK1 at anaphase and dephosphorylation, it is then phosphorylated by PLK1, leading to cytokinesis.

Sequence Similarities

Belongs to the MAP65/ASE1 family.

Tissue Specificity

Overexpressed in bladder cancer cells (PubMed:17409436).

Cellular localization

Alternative names

Protein regulator of cytokinesis 1, PRC1

swissprot:O43663 entrezGene:9055 omim:603484