PMID- 10557072
OWN - NLM
STAT- MEDLINE
DCOM- 19991210
LR  - 20131121
IS  - 0950-9232 (Print)
IS  - 0950-9232 (Linking)
VI  - 18
IP  - 43
DP  - 1999 Oct 21
TI  - Mouse ULK2, a novel member of the UNC-51-like protein kinases: unique features of
      functional domains.
PG  - 5850-9
AB  - The UNC-51 serine/threonine kinase of C. elegans plays an essential role in
      axonal elongation, and unc-51 mutants exhibit uncoordinated movements. We have
      previously identified mouse and human cDNAs encoding UNC-51-like kinase (ULK1).
      Here we report the identification and characterization of the second murine
      member of this kinase family, ULK2. Mouse ULK2 cDNA encodes a putative
      polypeptide of 1033 aa which has an overall 52% and 33% amino acid identity to
      ULK1 and UNC-51, respectively. ULKs and UNC-51 share a typical domain structure
      of an amino-terminal kinase domain, a central proline/serine rich (PS) domain,
      and a carboxy-terminal (C) domain. Northern blot analysis showed that ULK2 mRNA
      is widely expressed in adult tissues. In situ hybridization analysis indicated
      that ULK2 mRNA is ubiquitously localized in premature as well as mature neurons
      in developing nervous system. ULK2 gene was mapped to mouse chromosome 11B1.3 and
      rat chromosome 10q23 by FISH. HA-tagged ULK2 expressed in COS7 cells had an
      apparent molecular size of approximately 150 kDa and was autophosphorylated in
      vitro. Truncation mutants suggested that the autophosphorylation occurs in the PS
      domain. Although expression of ULK2 failed to rescue unc-51 mutant of C. elegans,
      a series of ULK2/UNC-51 chimeric kinases revealed that function of the kinase and
      PS domains are conserved among species, while the C domain acts in a
      species-specific manner. These results suggest that ULK2 is involved in a
      previously uncharacterized signaling pathway in mammalian cells.
FAU - Yan, J
AU  - Yan J
AD  - Helix Research Institute, 1532-3 Yana, Kisarazu, Chiba, 292-0812, Japan.
FAU - Kuroyanagi, H
AU  - Kuroyanagi H
FAU - Tomemori, T
AU  - Tomemori T
FAU - Okazaki, N
AU  - Okazaki N
FAU - Asato, K
AU  - Asato K
FAU - Matsuda, Y
AU  - Matsuda Y
FAU - Suzuki, Y
AU  - Suzuki Y
FAU - Ohshima, Y
AU  - Ohshima Y
FAU - Mitani, S
AU  - Mitani S
FAU - Masuho, Y
AU  - Masuho Y
FAU - Shirasawa, T
AU  - Shirasawa T
FAU - Muramatsu, M
AU  - Muramatsu M
LA  - eng
SI  - GENBANK/AB019577
PT  - Journal Article
PL  - England
TA  - Oncogene
JT  - Oncogene
JID - 8711562
RN  - 0 (Caenorhabditis elegans Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (RNA, Messenger)
RN  - EC 2.7.1.- (UNC-51 protein, C elegans)
RN  - EC 2.7.1.11 (Ulk2 protein, mouse)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Binding Sites
MH  - COS Cells
MH  - Caenorhabditis elegans
MH  - *Caenorhabditis elegans Proteins
MH  - Chromosome Mapping
MH  - Cloning, Molecular
MH  - DNA, Complementary
MH  - Gene Expression
MH  - Mice
MH  - Molecular Sequence Data
MH  - Protein Structure, Tertiary
MH  - Protein-Serine-Threonine Kinases/*chemistry/*genetics/metabolism
MH  - RNA, Messenger
MH  - Rats
MH  - Sequence Homology, Amino Acid
MH  - Tissue Distribution
EDAT- 1999/11/11 00:00
MHDA- 1999/11/11 00:01
CRDT- 1999/11/11 00:00
PHST- 1999/11/11 00:00 [pubmed]
PHST- 1999/11/11 00:01 [medline]
PHST- 1999/11/11 00:00 [entrez]
AID - 10.1038/sj.onc.1202988 [doi]
PST - ppublish
SO  - Oncogene. 1999 Oct 21;18(43):5850-9. doi: 10.1038/sj.onc.1202988.