Abstract
Phospholipase C (PLC)δ 1 shuttles between the nucleus and the cytoplasm. Here, we demonstrate that treatment of MDCK cells and PC12 cells with ionomycin causes nuclear accumulation of ectopically expressed and endogenous PLCδ 1, respectively, suggesting that signals that increase [Ca 2+] i trigger nuclear translocation. To clarify the molecular mechanisms involved in this translocation, we have examined whether PLCδ 1 binds with importins. PLCδ 1 interacted with importin β1 in a Ca 2+-dependent manner in vitro even in the absence of importin α. A PLCδ 1 mutant E341A, which lacks Ca 2+-binding to the catalytic core, did not show this interaction at any physiological Ca 2+ concentration and did not translocate into the nucleus after ionomycin treatment when expressed in MDCK cells. These results suggested that the nuclear import of PLCδ 1 is mediated by its Ca 2+-dependent interaction with importin β1.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
