TY - JOUR
T1 - (1)H, (15)N and (13)C resonance assignments of the conserved region in the middle domain of S. pombe Sin1 protein
AU - Kataoka, Saori
AU - Furuita, Kyoko
AU - Hattori, Yoshikazu
AU - Kobayashi, Naohiro
AU - Ikegami, Takahisa
AU - Shiozaki, Kazuhiro
AU - Fujiwara, Toshimichi
AU - Kojima, Chojiro
PY - 2015/4/1
Y1 - 2015/4/1
N2 - 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.
AB - 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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U2 - 10.1007/s12104-014-9550-6
DO - 10.1007/s12104-014-9550-6
M3 - Article
C2 - 24610629
AN - SCOPUS:84965084363
VL - 9
SP - 89
EP - 92
JO - Biomolecular NMR Assignments
JF - Biomolecular NMR Assignments
SN - 1874-2718
IS - 1
ER -