Evidence map›Paper›PMID 16934755›Full record

ArticleBiochemical and biophysical research communications2006

Phosphorylation of ErbB4 on Tyr1056 is critical for inhibition of colony formation by prostate tumor cell lines.

Richard M Gallo, Ianthe Bryant, Rachael Fry, Eric E Williams, David J Riese

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. The role of ErbB4 in cancer.Cellular oncology (Dordrecht, Netherlands) · 2020
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Nedd4 mediates ErbB4 JM-a/CYT-1 ICD ubiquitination and degradation in MDCK II cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2009
    Article
  11. Review
  12. Article
  13. Article
  14. Review
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

5 authors at 1 institution in 1 country.

Richard M GalloPurdue College of Pharmacy and Purdue Cancer Research Center, Purdue University, West Lafayette, IN 47907, USA.
Ianthe Bryant
Rachael Fry
Eric E Williams
David J Riese
Purdue University West Lafayette · US

Funding

Regulation of ErbB4 Signaling by Neuregulin IsoformsR01CA114209 · NCI · PURDUE UNIVERSITY · PI RIESE, DAVID J. · 2006 to 2010
$1.2M
Tumor Imaging Agents Directed Against ErbB2R21CA089274 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI RIESE, DAVID J. · 2001 to 2002
$300k
TUMOR CELL LINE PROLIFERATION, MOTILITY AND INVASIVENESSR21CA080770 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI RIESE, DAVID J. · 1999 to 2000
$114k
NCI NIH HHS R01 CA114209NCI NIH HHS R21CA080770NCI NIH HHS R21CA089274
6 · The paper itself

Abstract

We have previously demonstrated that the constitutively active Q646C mutant of the ErbB4 receptor tyrosine kinase inhibits colony formation by human prostate tumor cell lines. Here we use ErbB4 mutants to identify ErbB4 functions critical for inhibiting colony formation. A derivative of ErbB4 Q646 that lacks kinase activity fails to inhibit colony formation by prostate tumor cells. Likewise, an ErbB4 Q646C mutant in the context of the CT-b splicing isoform fails to inhibit colony formation. Mutation of tyrosine 1056 to phenylalanine abrogates inhibition of colony formation whereas an ErbB4 mutant that lacks all of the putative sites of tyrosine phosphorylation except for tyrosine 1056 still inhibits colony formation. Given that tyrosine 1056 is missing in the CT-b isoform, these results suggest that phosphorylation of tyrosine 1056 is critical for function. Indeed, an ErbB4 mutant that lacks kinase activity but has a glutamate phosphomimic residue substituted for tyrosine 1056 inhibits colony formation. Finally, 1-dimensional phosphopeptide mapping indicates that ErbB4 Q646C is phosphorylated on tyrosine 1056. These data suggest that phosphorylation of ErbB4 tyrosine 1056 is critical for coupling ErbB4 to prostate tumor suppression.

Indexed as

Gene Expression Regulation, NeoplasticAlternative SplicingCell Line, TumorCell ProliferationErbB ReceptorsGlutamic AcidHumansMalePhosphorylationProstatic NeoplasmsReceptor, ErbB-4Signal TransductionTyrosineERBB4 protein, humanErbB ReceptorsGlutamic AcidReceptor, ErbB-4Tyrosine

Identifiers

PMID16934755
PMCPMC1618953
OpenAlexW1971328908

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.