During the late G2/M transition, translation of PCNT mRNA is upregulated by an as yet unknown mechanism. The partially translated PCNT nascent polypeptide starts to interact with the dynein motor complex once the dynein light intermediate chain 1 (LIC1)-interacting domain in the N-terminal half of PCNT is synthesized and folded. It will be interesting to test if PLK1 phosphorylation of S1235 and S1241 within the LIC1-interacting domain initiates this PCNT-dynein interaction. Subsequently, this nascent polypeptide-dynein interaction allows the entire polysome, which is still actively translating PCNT mRNA, to be transported along the microtubule toward the centrosome. This co-translational targeting mechanism may maximize efficiency of PCNT production and delivery to the centrosome, prevent ectopic accumulation of PCNT outside of centrosomes, and/or facilitate integration of PCNT into the expanding PCM during early mitosis. It remains to be determined if other PCM components (e.g. CEP215) interact with PCNT co- and/or post-translationally.