Note: the first two authors contributed equally to this work.
PKCδ-dependent cleavage and nuclear translocation of annexin A1 by phorbol 12-myristate 13-acetate
Article first published online: 26 SEP 2003
European Journal of Biochemistry
Volume 270, Issue 20, pages 4089–4094, October 2003
How to Cite
Kim, Y. S., Ko, J., Kim, I. S., Jang, S.-W., Sung, H. J., Lee, H. J., Lee, S. Y., Kim, Y. and Na, D. S. (2003), PKCδ-dependent cleavage and nuclear translocation of annexin A1 by phorbol 12-myristate 13-acetate. European Journal of Biochemistry, 270: 4089–4094. doi: 10.1046/j.1432-1033.2003.03800.x
- Issue published online: 26 SEP 2003
- Article first published online: 26 SEP 2003
- (Received 15 July 2003, revised 17 August 2003, accepted 21 August 2003)
- annexin A1;
- nuclear translocation;
Annexin A1 (ANX-1), a calcium-dependent, phospholipid binding protein, is known to be involved in diverse cellular processes, including regulation of cell growth and differentiation, apoptosis, and inflammation. The mitogen phorbol 12-myristate 13-acetate (PMA) induces expression and phosphorylation of ANX-1. However, the roles of ANX-1 in PMA-induced signal transduction is unknown. Here, we study the cellular localization of ANX-1 in the PMA-induced signal transduction process. We have found that PMA induces the cleavage of ANX-1 in human embryonic kidney (HEK) 293 cells, and that the cleaved form of ANX-1 translocates to the nucleus. The PMA-induced nuclear translocation of ANX-1 was inhibited by the protein kinase C (PKC)δ-specific inhibitor rottlerin, indicating that PKCδ plays a role in nuclear translocation of the cleaved ANX-1. We propose a novel mechanism of PMA-induced translocation of ANX-1 to the nucleus that may participate in the regulation of cell proliferation and differentiation.