Evidence map›Paper›PMID 11751889›Full record

ArticleThe Journal of biological chemistry2002

Hsc/Hsp70 interacting protein (hip) associates with CXCR2 and regulates the receptor signaling and trafficking.

Guo-Huang Fan, Wei Yang, Jiqing Sai, Ann Richmond

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
5.0field-weighted citation impact, top 5% 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

25 citing papers in PubMed, 60 citations in OpenAlex.

  1. Evaluation of ST13 gene expression in colorectal cancer patients.Journal of Zhejiang University. Science. B · 2005
    Trial
  2. Article
  3. Article
  4. Review
  5. Review
  6. The STI1-domain is a flexible alpha-helical fold with a hydrophobic groove.Protein science : a publication of the Protein Society · 2021
    Article
  7. The Role of Heat Shock Protein 70 kDa in Asthma.Journal of asthma and allergy · 2020
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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  18. Article
  19. Review
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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

4 authors at 1 institution in 1 country.

Guo-Huang FanDepartment of Veterans Affairs, Nashville, Tennessee 37212-2637, USA.
Wei Yang
Jiqing Sai
Ann Richmond
Vanderbilt University · US

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
MELANOMA GROWTH STIMULATORY ACTIVITYR01CA034590 · NCI · VANDERBILT UNIVERSITY · PI RICHMOND, ANN · 1986 to 2017
$5.2M
BIOCHEMIISTRY OF A MELANOMA GROWTH STIMULATIONR23CA034590 · NCI · EMORY UNIVERSITY · PI RICHMOND, ANN · 1985 to 1985
–
BLRD VA IK6 BX005225NCI NIH HHS CA34590NCI NIH HHS CA68485NCI NIH HHS P30 CA068485NCI NIH HHS R01 CA034590
6 · The paper itself

Abstract

The ligand-induced trafficking of chemokine receptors plays a significant role in the regulation of inflammatory processes and human immunodeficiency infection. Although many chemokine receptors have been demonstrated to internalize through clathrin-coated vesicles, a process that involves the binding of arrestins to the receptors, accumulating evidence has suggested the possible existence of other regulators. In a yeast two-hybrid screening using the C-terminal domain of CXCR2 as a bait, the Hsc70-interacting protein (Hip) was identified to interact with CXCR2. Hip binds CXCR2 through its C-terminal domain binding to the C-terminal leucine-rich domain (KILAIHGLI) of CXCR2. Hip associates with CXCR2 or CXCR4 in intact cells, and agonist stimulation increases the association. Mutation of the Ile-Leu motif in the C-terminal domain of CXCR2 blocks the agonist-dependent association of the mutant receptor with Hip. Overexpression of a tetratricopeptide repeat (TPR) deletion mutant form of Hip (Delta TPR), which is unable to bind Hsc70 (Prapapanich, V., Chen, S., Nair, S. C., Rimerman, R. A., and Smith, D. F. (1996) Mol. Endocrinol. 10, 420-431), but retains the ability to bind CXCR2, does not affect CXCR2-mediated mitogen-activated protein kinase activation. However, overexpression of Delta TPR significantly attenuates the agonist-induced internalization of CXCR2 and CXCR4 and attenuates CXCR2-mediated chemotaxis. These findings open the possibility for regulation of chemokine receptor signaling and trafficking by protein chaperone molecules.

Indexed as

Tumor Suppressor ProteinsAnimalsBinding SitesCarrier ProteinsCell LineGene LibraryHumansKineticsLeukemia, Basophilic, AcuteLigandsMolecular ChaperonesPeptide FragmentsRatsReceptors, CXCR4Receptors, Interleukin-8BRecombinant ProteinsCarrier ProteinsLigandsMolecular ChaperonesPeptide FragmentsReceptors, CXCR4Receptors, Interleukin-8BRecombinant ProteinsST13 protein, humanTumor Suppressor Proteins

Identifiers

PMID11751889
PMCPMC2665275
OpenAlexW2051456620

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.