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Background
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Stk38,also known as NUCLEAR DBF2-RELATED PROTEIN, contains 1 protein kinase domain that interacts with mob1 and mob2.The homodimeric s100b binds to two molecules of stk38. It is ubiquitously expressed with highest levels observed in peripheral blood leukocytes. Stk38 activated by binding of s100b which releases autoinhibitory n-lobe interactions, enabling atp to bind and the autophosphorylation of ser-281. thr-444 then undergoes calcium- dependent phosphorylation by an upstream kinase. Interactions between phosphorylated thr-444 and the n-lobe promote additional structural changes that complete the activation of the kinase. Autoinhibition is also released by the binding of mob1/mobkl1a and mob2/hcca2 to the n-terminal of stk38.
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Background
References
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- Devroe, E., et al., J. Biol. Chem. 279(23):24444-24451 (2004).
- Tamaskovic, R., et al., J. Biol. Chem. 278(9):6710-6718 (2003).
- Tripodis, N., et al., Genome Res. 8(6):631-643 (1998).
- Millward, T., et al., Proc. Natl. Acad. Sci. U.S.A. 92(11):5022-5026 (1995).
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