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 language | English |
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Pages (from-to) | 117-121 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 399 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 1996 Dec 9 |
Externally published | Yes |
Keywords
- Dimerization
- LIM motif
- LIMK
- Protein kinase
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology