(1)H, (15)N and (13)C resonance assignments of the conserved region in the middle domain of S. pombe Sin1 protein

Saori Kataoka; Kyoko Furuita; Yoshikazu Hattori; Naohiro Kobayashi; Takahisa Ikegami; Kazuhiro Shiozaki; Toshimichi Fujiwara; Chojiro Kojima

doi:10.1007/s12104-014-9550-6

(1)H, (15)N and (13)C resonance assignments of the conserved region in the middle domain of S. pombe Sin1 protein

Saori Kataoka, Kyoko Furuita, Yoshikazu Hattori, Naohiro Kobayashi, Takahisa Ikegami, Kazuhiro Shiozaki, Toshimichi Fujiwara, Chojiro Kojima

Research output: Contribution to journal › Article

2 Scopus citations

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 (1)H, (13)C and (15)N 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.

Original language	English (US)
Pages (from-to)	89-92
Number of pages	4
Journal	Biomolecular NMR Assignments
Volume	9
Issue number	1
DOIs	https://doi.org/10.1007/s12104-014-9550-6
State	Published - Apr 1 2015
Externally published	Yes

ASJC Scopus subject areas

Medicine(all)

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Kataoka, S., Furuita, K., Hattori, Y., Kobayashi, N., Ikegami, T., Shiozaki, K., Fujiwara, T., & Kojima, C. (2015). (1)H, (15)N and (13)C resonance assignments of the conserved region in the middle domain of S. pombe Sin1 protein. Biomolecular NMR Assignments, 9(1), 89-92. https://doi.org/10.1007/s12104-014-9550-6

(1)H, (15)N and (13)C resonance assignments of the conserved region in the middle domain of S. pombe Sin1 protein. / Kataoka, Saori; Furuita, Kyoko; Hattori, Yoshikazu; Kobayashi, Naohiro; Ikegami, Takahisa; Shiozaki, Kazuhiro; Fujiwara, Toshimichi; Kojima, Chojiro.

In: Biomolecular NMR Assignments, Vol. 9, No. 1, 01.04.2015, p. 89-92.

Research output: Contribution to journal › Article

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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 (1)H, (13)C and (15)N 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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