Evidence map›Paper›PMID 18635666›Full record

ArticleMolecular endocrinology (Baltimore, Md.)2008

Analysis of the calcium-dependent regulation of proline-rich tyrosine kinase 2 by gonadotropin-releasing hormone.

Jianjun Xie, Krystal H Allen, Amelia Marguet, Kathie A Berghorn, Stuart P Bliss, Amy M Navratil, Jun Lin Guan, Mark S Roberson

Open access · bronzeAbstract read
In one paragraph

Article in Molecular endocrinology (Baltimore, Md.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  4. Review
  5. Review
  6. Membrane translocation of TRPC6 channels and endothelial migration are regulated by calmodulin and PI3 kinase activation.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  7. Article
  8. Article
  9. Review
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  12. Review
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  15. Article
  16. The biology of gonadotroph regulation.Current opinion in endocrinology, diabetes, and obesity · 2009
    Review
  17. 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

8 authors at 2 institutions in 1 country.

Jianjun XieDepartment of Biomedical Sciences, Cornell University, Ithaca, New York 14853, USA.
Krystal H Allen
Amelia Marguet
Kathie A Berghorn
Stuart P Bliss
Amy M Navratil
Jun Lin Guan
Mark S Roberson
Cornell University · USUniversity of Michigan–Ann Arbor · US

Funding

Molecular analysis of GnRH hormone actionR01HD034722 · NICHD · CORNELL UNIVERSITY ITHACA · PI ROBERSON, MARK S · 2003 to 2012
$3.0M
Reproductive Sciences and Genomics Training ProgramT32HD052471 · NICHD · CORNELL UNIVERSITY · PI ROBERSON, MARK S · 2007 to 2016
$2.0M
NICHD NIH HHS R01 HD034722NICHD NIH HHS R01 HD34722NICHD NIH HHS T32 HD052471
6 · The paper itself

Abstract

Calcium influx through L-type voltage-gated calcium channels (VGCC) is required for ERK activation induced by GnRH in pituitary gonadotropes. The current studies investigate VGCC-sensitive catalytic activities that may lie upstream of ERKs within the GnRH signaling network. Ion exchange fractionation of alphaT3-1 cell lysates subjected to anti-phosphotyrosine Western blot analysis revealed a nifedipine-sensitive activity that colocalized with proline-rich tyrosine kinase (Pyk) 2 immunoreactivity. Phosphorylated Pyk2 was present in alphaT3-1 cells after GnRH agonist administration for a time course that lasted up to 4 h. Pyk2 phosphorylation was also evident in gonadotropes in vivo after administration of a bolus of GnRH. Knockdown of Pyk2 using specific small interfering RNAs revealed that Pyk2 contributed to modulation of GnRH-induced ERK but not c-Jun N-terminal kinase activation. Using pharmacological approaches, calmodulin (Cam) was also demonstrated to be required for the phosphorylation of Pyk2. Pyk2 was shown to bind specifically to a Cam agarose affinity column in a calcium-dependent manner, suggesting Cam and Pyk2 are capable of forming a complex. Specific mutation of a putative Cam binding motif within the catalytic domain of Pyk2 blocked association with Cam and uncoupled Pyk2's ability to activate ERK-dependent gene transcription. Thus, GnRH induces Pyk2 tyrosine phosphorylation dependent upon calcium flux within gonadotropes. Furthermore, association of Pyk2 and Cam may be required to mediate the effects of calcium on Pyk2 phosphorylation and subsequent activation of ERKs by GnRH.

Indexed as

Amino Acid SequenceAnimalsCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium ChannelsCalmodulinCatalytic DomainCell LineEnzyme ActivationExtracellular Signal-Regulated MAP KinasesFocal Adhesion Kinase 2Focal Adhesion Protein-Tyrosine KinasesGonadotropin-Releasing HormoneHumansMiceMolecular Sequence DataCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium ChannelsCalmodulinExtracellular Signal-Regulated MAP KinasesFocal Adhesion Kinase 2Focal Adhesion Protein-Tyrosine KinasesGonadotropin-Releasing HormoneRNA, Small Interfering

Identifiers

PMID18635666
PMCPMC2582532
OpenAlexW1965648238

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.