Self-association of LIM-kinase 1 mediated by the interaction between an N-terminal LIM domain and a C-terminal kinase domain

Junji Hiraoka, Ichiro Okano, Osamu Higuchi, Neng Yang, Kensaku Mizuno

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)

Abstract

LIM-kinase 1 (LIMK1) and 2 (LIMK2) are members of a novel class of protein kinases containing two LIM motifs at the N-terminus. The LIM motif is thought to be involved in protein-protein interactions. We report here evidence that LIMK1 self-associates and also associates with LIMK2. In vivo and in vitro binding analyses using variously deleted mutants of LIMK1 revealed that the self-association of LIMK1 was caused by interaction between the N-terminal LIM domain and the C-terminal kinase domain. The association of LIMK1 with itself and with LIMK2 is important for understanding how activities and functions of LIMK family kinases are regulated.

Original languageEnglish
Pages (from-to)117-121
Number of pages5
JournalFEBS Letters
Volume399
Issue number1-2
DOIs
Publication statusPublished - 1996 Dec 9
Externally publishedYes

Keywords

  • Dimerization
  • LIM motif
  • LIMK
  • Protein kinase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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