小鼠ULK1的鉴定，一种与秀丽隐杆线虫UNC-51结构相关的新型蛋白激酶。

Identification of mouse ULK1, a novel protein kinase structurally related to C. elegans UNC-51.

作者信息

Yan J, Kuroyanagi H, Kuroiwa A, Matsuda Y, Tokumitsu H, Tomoda T, Shirasawa T, Muramatsu M

机构信息

Helix Research Institute, Chiba, Japan.

出版信息

Biochem Biophys Res Commun. 1998 May 8;246(1):222-7. doi: 10.1006/bbrc.1998.8546.

DOI:10.1006/bbrc.1998.8546

PMID:9600096

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 approximately 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.

摘要

从小鼠中克隆出一种与秀丽隐杆线虫丝氨酸/苏氨酸激酶UNC-51相关的新型蛋白激酶。UNC-51样激酶（ULK）1由一个1051个氨基酸的cDNA编码，计算分子量为113 kDa。ULK1与UNC-51的比较显示，在氨基末端激酶结构域中保守性最高，其次是富含脯氨酸/丝氨酸（PS）的结构域和保守的羧基末端（C）结构域。通过荧光原位杂交，ULK1 mRNA在各种组织中表达，并定位于小鼠5F染色体和大鼠12q16.3染色体。带有HA标签的ULK1在COS7细胞中表达为约150 kDa的蛋白质，并在体外其PS结构域中发生自磷酸化。我们提出，ULK1、UNC-51和酵母蛋白激酶Apg1p构成了一个新型的蛋白激酶亚家族，该亚家族在真核生物中结构保守。