Evidence map›Paper›PMID 16705160›Full record

ArticleMolecular and cellular biology2006

Phosphorylation of Jak2 on Ser(523) inhibits Jak2-dependent leptin receptor signaling.

Ryoko Ishida-Takahashi, Felicia Rosario, Yusong Gong, Keely Kopp, Zlatina Stancheva, Xiaohong Chen, Edward P Feener, Martin G Myers

Erratum issuedAbstract read
In one paragraph

Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
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

30 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Biology and significance of the JAK/STAT signalling pathways.Growth factors (Chur, Switzerland) · 2012
    Review
  14. Janus kinase 3: the controller and the controlled.Acta biochimica et biophysica Sinica · 2012
    Review
  15. JAK Kinases in Health and Disease: An Update.The open rheumatology journal · 2012
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

8 authors.

Ryoko Ishida-TakahashiResearch Division, Joslin Diabetes Center, 1 Joslin Place, Boston, MA 02215, USA.
Felicia Rosario
Yusong Gong
Keely Kopp
Zlatina Stancheva
Xiaohong Chen
Edward P Feener
Martin G Myers

Funding

SPECIAL ASSAY COREP30DK036836 · NIDDK · JOSLIN DIABETES CENTER · PI JEAN E. SCHAFFER · 1986 to 2026
$50.5M
PUBLIC HEALTH DEMONSTRATIONP60DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MYERS, MARTIN G · 1985 to 2012
$26.5M
MOLECULAR DETERMINANTS OF LEPTIN RECEPTOR/JAK2 SIGNALINGR01DK056731 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MYERS, MARTIN G · 1999 to 2025
$6.0M
Mechanisms of Leptin Receptors Signal AttenuationR01DK057768 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MYERS, MARTIN G, SIMERLY, RICHARD B · 2000 to 2012
$5.3M
Molecular Mechanisms of Leptin Receptor/Jak2 ActionR37DK056731 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MYERS, MARTIN G · 2008 to 2017
$3.5M
NIDDK NIH HHS DK36836NIDDK NIH HHS DK56731NIDDK NIH HHS P30 DK036836NIDDK NIH HHS P60 DK020572NIDDK NIH HHS P60 DK20572NIDDK NIH HHS R01 DK056731NIDDK NIH HHS R01 DK057768NIDDK NIH HHS R37 DK056731
6 · The paper itself

Abstract

The leptin receptor, LRb, and other cytokine receptors are devoid of intrinsic enzymatic activity and rely upon the activity of constitutively associated Jak family tyrosine kinases to mediate intracellular signaling. In order to clarify mechanisms by which Jak2, the cognate LRb-associated Jak kinase, is regulated and mediates downstream signaling, we employed tandem mass spectroscopic analysis to identify phosphorylation sites on Jak2. We identified Ser523 as the first-described site of Jak2 serine phosphorylation and demonstrated that this site is phosphorylated on Jak2 from intact cells and mouse spleen. Ser523 was highly phosphorylated in HEK293 cells independently of LRb-Jak2 activation, suggesting a potential role for the phosphorylation of Ser523 in the regulation of LRb by other pathways. Indeed, mutation of Ser523 sensitized and prolonged signaling by Jak2 following activation by the intracellular domain of LRb. The effect of Ser523 on Jak2 function was independent of Tyr570-mediated inhibition. Thus, the phosphorylation of Jak2 on Ser523 inhibits Jak2 activity and represents a novel mechanism for the regulation of Jak2-dependent cytokine signaling.

Indexed as

Signal TransductionAnimalsEnzyme ActivationGene Expression Regulation, EnzymologicGlutamic AcidHumansJanus Kinase 2Mass SpectrometryMiceMutationPhosphorylationPhosphoserineProtein-Tyrosine KinasesProto-Oncogene ProteinsReceptors, Cell SurfaceReceptors, LeptinGlutamic AcidJAK2 protein, humanJak2 protein, mouseJanus Kinase 2LEPR protein, humanleptin receptor, mousePhosphoserineProtein-Tyrosine KinasesProto-Oncogene ProteinsReceptors, Cell SurfaceReceptors, Leptin

Identifiers

PMID16705160
PMCPMC1489076

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.