TY - JOUR
T1 - Identification of mouse ULK1, a novel protein kinase structurally related to C. elegans UNC-51
AU - Yan, Jin
AU - Kuroyanagi, Hidehito
AU - Kuroiwa, Asato
AU - Matsuda, Yo Ichi
AU - Tokumitsu, Hiroshi
AU - Tomoda, Toshifumi
AU - Shirasawa, Takuji
AU - Muramatsu, Masa Aki
N1 - Funding Information:
Helix Research Institue is supported by The Japan Key Technology Center, Chugai Pharmaceutical Co., Fujisawa Pharmaceutical Co., Hitachi Co., Japan Associated Finance Co., Kyowa Hakko Kogyo Co., Mitsubishi Chemical Co., Sumitomo Chemical Co., Taisho Pharmaceutical Co., Yamanouchi Pharmaceutical Co., and Yoshitomi Pharmaceutical Co.
PY - 1998/5/8
Y1 - 1998/5/8
N2 - A novel protein kinase related to the C. elegans serine/threonine kinase UNC-51 was cloned from mouse. The UNC-51-Like Kinase (ULK)1 is encoded by a cDNA of 1051 amino acids with calculated MW of 113 kDa. Comparison of the ULK1 and UNC-51 shows the highest conservation in the amino-terminal kinase domain, which is followed by a proline/serine-rich (PS) domain and a conserved carboxyl-terminal (C) domain. ULK1 mRNA is expressed in various tissues, and is mapped to mouse chromosome 5F and rat chromosome 12q16.3, by fluorescent in situ hybridization. HA-tagged ULK1 is expressed as a protein of ~150 kDa in COS7 cells and is auto-phosphorylated in vitro in its PS domain. We propose that ULK1, UNC-51 and a yeast protein kinase Apg1p comprise a novel subfamily of protein kinase, which is structurally conserved among eukaryotes.
AB - A novel protein kinase related to the C. elegans serine/threonine kinase UNC-51 was cloned from mouse. The UNC-51-Like Kinase (ULK)1 is encoded by a cDNA of 1051 amino acids with calculated MW of 113 kDa. Comparison of the ULK1 and UNC-51 shows the highest conservation in the amino-terminal kinase domain, which is followed by a proline/serine-rich (PS) domain and a conserved carboxyl-terminal (C) domain. ULK1 mRNA is expressed in various tissues, and is mapped to mouse chromosome 5F and rat chromosome 12q16.3, by fluorescent in situ hybridization. HA-tagged ULK1 is expressed as a protein of ~150 kDa in COS7 cells and is auto-phosphorylated in vitro in its PS domain. We propose that ULK1, UNC-51 and a yeast protein kinase Apg1p comprise a novel subfamily of protein kinase, which is structurally conserved among eukaryotes.
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U2 - 10.1006/bbrc.1998.8546
DO - 10.1006/bbrc.1998.8546
M3 - Article
C2 - 9600096
AN - SCOPUS:0032495976
VL - 246
SP - 222
EP - 227
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -