PKCδ-dependent cleavage and nuclear translocation of annexin A1 by phorbol 12-myristate 13-acetate

Yoon S. Kim, Jesang Ko, In S. Kim, Sung Wuk Jang, Ho J. Sung, Hye J. Lee, Si Y. Lee, Youngho Kim, Doe S. Na

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26 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)4089-4094
Number of pages6
JournalEuropean Journal of Biochemistry
Issue number20
Publication statusPublished - 2003 Oct
Externally publishedYes


  • Annexin A1
  • Cleavage
  • Nuclear translocation
  • PKCδ
  • PMA

ASJC Scopus subject areas

  • Biochemistry


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