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Nuclear entry of circadian oscillatory gene products is a key step for thegeneration of a 24-hr cycle of the biological clock. We have examinednuclear import of clock proteins of the mammalian period gene family andthe effect of serum shock, which induces a synchronous clock in culturedcells. Previously, mCRY1 and mCRY2 have been found to complex with PERproteins leading to nuclear import. Here we report that nucleartranslocation of mPER1 and mPER2 (1) involves physical interactions withmPER3, (2) is accelerated by serum treatment, and (3) still occurs inmCry1/mCry2 double-deficient cells lacking a functional biological clock.Moreover, nuclear localization of endogenous mPER1 was observed incultured mCry1/mCry2 double-deficient cells as well as in the liver andthe suprachiasmatic nuclei (SCN) of mCry1/mCry2 double-mutant mice. Thisindicates that nuclear translocation of at least mPER1 also can occurunder physiological conditions (i.e., in the intact mouse) in the absenceof any CRY protein. The mPER3 amino acid sequence predicts the presence ofa cytoplasmic localization domain (CLD) and a nuclear localization signal(NLS). Deletion analysis suggests that the interplay of the CLD and NLSproposed to regulate nuclear entry of PER in Drosophila is conserved inmammals, but with the novel twist that mPER3 can act as the dimerizingpartner

Dimerization and nuclear entry of mPER proteins in mammalian cells