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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Autophagy-Related Protein-1 Homolog
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Base Sequence
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Caenorhabditis elegans / genetics*
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Caenorhabditis elegans Proteins*
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Chromosome Mapping
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Cloning, Molecular
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DNA, Complementary / genetics
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Gene Expression
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Helminth Proteins / genetics*
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In Situ Hybridization, Fluorescence
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Mice
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Molecular Sequence Data
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Molecular Weight
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Phosphorylation
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Protein Kinases / chemistry
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Protein Kinases / genetics*
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Protein Serine-Threonine Kinases / chemistry
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Protein Serine-Threonine Kinases / genetics*
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Rats
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Sequence Homology, Amino Acid
Substances
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Caenorhabditis elegans Proteins
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DNA, Complementary
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Helminth Proteins
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RNA, Messenger
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Protein Kinases
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UNC-51 protein, C elegans
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Autophagy-Related Protein-1 Homolog
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Protein Serine-Threonine Kinases
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Ulk1 protein, mouse