Identification of the dual specificity and the functional domains of the cardiac-specific protein kinase TNNI3K

Molecular cloning of cardiac troponin I-interacting kinase (TNNI3K), a novel cardiac-specific protein kinase containing seven N-terminal ankyrin (ANK) repeats followed by a protein kinase domain and a C-terminal Ser-rich domain, has previously been reported. In the present study, we show that the C-...

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Bibliographic Details
Published in:General physiology and biophysics 2007-06, Vol.26 (2), p.104-109
Main Authors: Feng, Y, Cao, H Q, Liu, Z, Ding, J F, Meng, X M
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Cell Line, Transformed
Cloning, Molecular
Dimerization
Enzyme Activation
Gene Expression Regulation
Humans
MAP Kinase Kinase Kinases - chemistry
MAP Kinase Kinase Kinases - metabolism
Myocytes, Cardiac - enzymology
Phosphorylation
Protein Multimerization
Protein Structure, Tertiary
Protein-Serine-Threonine Kinases - metabolism
Protein-Tyrosine Kinases - metabolism
Serine - chemistry
Serine - metabolism
Structure-Activity Relationship
Substrate Specificity
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Summary:Molecular cloning of cardiac troponin I-interacting kinase (TNNI3K), a novel cardiac-specific protein kinase containing seven N-terminal ankyrin (ANK) repeats followed by a protein kinase domain and a C-terminal Ser-rich domain, has previously been reported. In the present study, we show that the C-terminal functional region of TNNI3K negatively regulates the kinase activity, and the N-terminal ANK domain is necessary for autophosphorylation. An in vitro kinase assay shows that TNNI3K exhibits dual-specific kinase activity and forms dimers or oligomers that may be necessary for its activation.
ISSN:0231-5882