Protein-protein interaction of zinc finger LIM domains with protein kinase C

Shun'ichi Kuroda, Chiharu Tokunaga, Yoshimoto Kiyohara, Osamu Higuchi, Hiroaki Konishi, Kensaku Mizuno, Gordon N. Gill, Ushio Kikkawa

Research output: Contribution to journalArticlepeer-review

218 Citations (Scopus)


The LIM domain comprising two zinc-finger motifs is found in a variety of proteins and has been proposed to direct protein-protein interactions. During the identification of protein kinase C (PKC)-interacting proteins by a yeast two-hybrid assay, a novel protein containing three LIM domains, designated ENH, was shown to associate with PKC in an isoform-specific manner. Deletion analysis demonstrated that any single LIM domain of ENH associates with the NH2-terminal region of PKC. ENH associated with PKC in COS-7 cells and was phosphorylated by PKC in vitro. Upon treatment of the cells with phorbol ester, ENH in the membrane fraction was translocated to the cytosol fraction in vivo. Other LIM domain-containing proteins, such as Enigma and LIM-kinase 1, also interacted with PKC through their LIM domains. These results suggest that the LIM domain is one of the targets of PKC and that the LIM-PKC interaction may shed light on undefined roles of LIM domain- containing proteins.

Original languageEnglish
Pages (from-to)31029-31032
Number of pages4
JournalJournal of Biological Chemistry
Issue number49
Publication statusPublished - 1996
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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