Abstract
SAPK-interacting protein 1 (Sin1) is an important component of the target of rapamycin (TOR) complex 2 (TORC2). TOR is a serine/threonine-specific protein kinase and forms functionally distinct protein complexes referred to as TORC1 and TORC2. TORC2, conserved from yeast to humans, phosphorylates AGC-family protein kinases and has many cellular functions including the regulation of actin cytoskeleton. The Sin1 subunit of TORC2 is required for the binding of TORC2 to substrates, and the conserved region in the middle (CRIM) domain of Sin1 is important in the substrate recognition of TORC2. Here, we report on the 1H, 13C and 15N resonance assignments of fission yeast Schizosaccharomyces pombe Sin1 (amino acids 247–400) (Sin1CRIM), which possesses the CRIM domain. These data contribute toward the structure determination of Sin1CRIM and an understanding of the interactions of Sin1CRIM with substrates of TORC2.
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Acknowledgments
We thank Yuki Nishigaya for the mass spectrometry, and Izuru Ohki, Shinichi Murayama and Hisashi Tatebe for helpful comments. This work was supported in part by grants from MEXT/JSPS KAKENHI, TPRP, Platform for Drug Discovery, Informatics, and Structural Life Science to K.S., T.F. and C.K., and Grants-in-Aid for JSPS Fellows to S.K. and K.F.
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Kataoka, S., Furuita, K., Hattori, Y. et al. 1H, 15N and 13C resonance assignments of the conserved region in the middle domain of S. pombe Sin1 protein. Biomol NMR Assign 9, 89–92 (2015). https://doi.org/10.1007/s12104-014-9550-6
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DOI: https://doi.org/10.1007/s12104-014-9550-6