Description: Alternative splicing removes the cyclin-dependent kinase (CDK) phosphorylation motif of Isoform Cenexin 1 of Outer dense fiber protein 2 (ODF2), abrogating binding to Cyclin-dependent kinase 1 (CDK1). This phosphorylation is required for the recruitment of Serine/threonine-protein kinase PLK1 (PLK1). The C-terminal extension of Isoform Cenexin 1 of Outer dense fiber protein 2 (ODF2) has the ability to distinctly localise to mother centriole whereas the splice variant (e.g. Isoform Cenexin 1 of Outer dense fiber protein 2 (ODF2)), which does not have this extension, permits ODF2 to associate with sperm tail.
Participants: (1) Isoform Cenexin 1 of Outer dense fiber protein 2 (ODF2) (2) Cyclin-dependent kinase 1 (CDK1)
(1) Plk1-dependent and -independent roles of an ODF2 splice variant, hCenexin1, at the centrosome of somatic cells.Soung et al. Dev. Cell (2009)
Other switches involving participantsCyclin-dependent kinase 1 (CDK1) - 1 more (view)Other switches involving interfacesProtein kinase domain - 35 more (view)MOD_CDK_1 - 3 more (view)
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