Abstract
Serine/threonine kinases of the nuclear Dbf2-related (NDR) family are highly conserved throughout the eukaryotic world. Members of this kinase family are implicated in various aspects of the regulation of cell division and cell morphology. It has been shown that the function of several NDR kinases is dependent on proteins of the Mob (MPS one binder) family. MOB proteins are highly conserved throughout the eukaryotic world as well, which indicates the existence of a novel conserved signalling pathway. The current work focuses on the mechanism of activation of human NDR kinase by the human MOB1 protein. hMOB1 directly activates NDR by binding to the Nterminal domain of NDR, thereby hMOB1 acts as a kinase activating subunit of NDR kinase. The binding induces the release of an autoinhibition caused by an autoinhibitory sequence (AIS) and leads to increased phosphorylation of NDR kinase on the two important regulatory phosphorylation sites Ser-281 and Thr-444.
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