Evidence map›Paper›PMID 10557072›Full record

ArticleOncogene1999

Mouse ULK2, a novel member of the UNC-51-like protein kinases: unique features of functional domains.

J Yan, H Kuroyanagi, T Tomemori, N Okazaki, K Asato, Y Matsuda, Y Suzuki, Y Ohshima, S Mitani, Y Masuho and 2 more

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
0.1field-weighted citation impact, top 63% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

51 citing papers in PubMed, 90 citations in OpenAlex.

  1. Physiological functions of ULK1/2.Journal of molecular biology · 2024
    Review
  2. Article
  3. Toxics · 2023
    Review
  4. Article
  5. Review
  6. Article
  7. ULK overexpression mitigates motor deficits and neuropathology in mouse models of Machado-Joseph disease.Molecular therapy : the journal of the American Society of Gene Therapy · 2022
    Article
  8. Review
  9. GSK3B induces autophagy by phosphorylating ULK1.Experimental & molecular medicine · 2021
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Autophagy core machinery: overcoming spatial barriers in neurons.Journal of molecular medicine (Berlin, Germany) · 2016
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 5 institutions in 1 country.

J YanHelix Research Institute, 1532-3 Yana, Kisarazu, Chiba, 292-0812, Japan.
H Kuroyanagi
T Tomemori
N Okazaki
K Asato
Y Matsuda
Y Suzuki
Y Ohshima
S Mitani
Y Masuho
T Shirasawa
M Muramatsu
Tokyo Metropolitan Institute of Gerontology · JPNagoya University · JPJapan Science and Technology Agency · JPKyushu University · JPTokyo Women's Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Caenorhabditis elegans ProteinsAmino Acid SequenceAnimalsBase SequenceBinding SitesCaenorhabditis elegansChromosome MappingCloning, MolecularCOS CellsDNA, ComplementaryGene ExpressionMiceMolecular Sequence DataProtein Serine-Threonine KinasesProtein Structure, TertiaryRatsCaenorhabditis elegans ProteinsDNA, ComplementaryProtein Serine-Threonine KinasesRNA, MessengerUlk2 protein, mouseUNC-51 protein, C elegans

Identifiers

PMID10557072
OpenAlexW2063650770

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.