Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 222-227 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 246 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - May 8 1998 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Identification of mouse ULK1, a novel protein kinase structurally related to C. elegans UNC-51. / Yan, Jin; Kuroyanagi, Hidehito; Kuroiwa, Asato; Matsuda, Yo Ichi; Tokumitsu, Hiroshi; Tomoda, Toshifumi; Shirasawa, Takuji; Muramatsu, Masa Aki.
In: Biochemical and Biophysical Research Communications, Vol. 246, No. 1, 08.05.1998, p. 222-227.Research output: Contribution to journal › Article
}
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
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
VL - 246
SP - 222
EP - 227
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -