CEP68 Antibody - #DF9364

Involved in maintenance of centrosome cohesion, probably as part of a linker structure which prevents centrosome splitting. Required for localization of CDK5RAP2 to the centrosome during interphase.

Phosphorylation by PLK1 is required for binding to BTRC in prometaphase. Phosphorylated directly or indirectly by NEK2. NEK2-mediated phosphorylation promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis.

Ubiquitinated and targeted for proteasomal degradation in early mitosis by the SCF(BTRC) and/or SCF(FBXW11) E3 ubiquitin-protein ligase complexes. Degradation is complete by prometaphase and is required for removal of CDK5RAP2 from the peripheral pericentriolar material and subsequent centriole separation.

Cytoplasm>Cytoskeleton>Microtubule organizing center>Centrosome.
Note: Localizes to thin fibers protruding away from the proximal ends of the two centrioles. Dissociates from interphase centrosomes at the onset of mitosis.

Interacts with CNTLN; the interaction recruits CEP68 to the centrosome. Interacts with the SCF(FBXW11) complex which contains SKP1, CUL1 and FBXW11; the interaction is probably mediated by FBXW11 and the complex also contains CDK5RAP2 and PCNT. Also interacts with F-box protein BTRC. Interacts with serine/threonine-protein kinase PLK1; the interaction leads to phosphorylation of CEP68 and its subsequent degradation. Interacts with NEK2; the interaction leads to phosphorylation of CEP68.