Published online Apr 23, 2012. doi: 10.5494/wjh.v2.i2.22
Revised: October 24, 2011
Accepted: March 5, 2012
Published online: April 23, 2012
TNNI3K is a cardiac-specific and cardiac troponin I (cTnI)-interacting MAP kinase, known to play important roles in promoting cardiac differentiation, maintenance of beating rhythm and contractual force. The molecular structure of TNNI3K contains three kinds of domain: a seven or ten NH2-terminal ankyrin repeat domain followed by a protein kinase domain and a COOH-terminal serine-rich domain. There are many binding sites in the structure of TNNI3K for binding to ATP, magnesium, nucleotide, protein kinase C, antioxidant protein 1 (AOP-1) and cTnI, indicating TNNI3K has many interacting partners. This review summarizes the evidence, hypothesis and significance of TNNI3K interacting with TNNI3 and its other putative interaction partners. From the literature, the interaction partners of TNNI3K are divided into 2 types following their phenotypic pattern of functions, positive interaction (to increase the cardiac performance) or negative interaction (to suppress the cardiac performance). Following their binding sites, it also can be divided into other 2 types: binding to C-terminal domain (e.g., cTnI) or binding to both ankyrin repeat domain and C-terminal domains (AOP-1). To date, a well understood partner of TNNI3K is cTnI, from the molecular structure, physiological function, mechanisms and its significance in some physiological and pathophysiological conditions. There are many reasons to believe that, with more understanding on the TNNI3K interacting with its partners, we can understand more roles of TNNI3K in some cardiac diseases.