Evidence map›Paper›PMID 21852394›Full record

ArticleDevelopment (Cambridge, England)2011

Distinct and mutually inhibitory binding by two divergent β-catenins coordinates TCF levels and activity in C. elegans.

Xiao-Dong Yang, Shuyi Huang, Miao-Chia Lo, Kota Mizumoto, Hitoshi Sawa, Wenqing Xu, Scott Robertson, Rueyling Lin

Open access · bronzeAbstract read
In one paragraph

Article in Development (Cambridge, England), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. β-Catenin-related protein WRM-1 is a multifunctional regulatory subunit of the LIT-1 MAPK complex.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. TCF/LEFs and Wnt signaling in the nucleus.Cold Spring Harbor perspectives in biology · 2012
    Review
  14. Review
  15. Article
  16. β-catenin-driven binary cell fate decisions in animal development.Wiley interdisciplinary reviews. Developmental biology
    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

8 authors at 5 institutions in 2 countries.

Xiao-Dong YangDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Shuyi Huang
Miao-Chia Lo
Kota Mizumoto
Hitoshi Sawa
Wenqing Xu
Scott Robertson
Rueyling Lin
The University of Texas Southwestern Medical Center · USNational Institute of Genetics · JPStanford University · USUniversity of California, San Diego · USUniversity of Washington · US

Funding

Transcriptional Regulation by the Wnt Effector POP-1R01HD037933 · NICHD · UT SOUTHWESTERN MEDICAL CENTER · PI LIN, RUEYLING · 2000 to 2014
$4.5M
REPROGRAMMING BY mRNA CLEARANCE: THE MAT-TO-ZYG TRANSITIONR01GM084198 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI LIN, RUEYLING, ZHANG, MICHAEL Q · 2009 to 2018
$2.8M
NICHD NIH HHS HD37933NICHD NIH HHS R01 HD037933NIGMS NIH HHS GM84198NIGMS NIH HHS R01 GM084198
6 · The paper itself

Abstract

Wnt target gene activation in C. elegans requires simultaneous elevation of β-catenin/SYS-1 and reduction of TCF/POP-1 nuclear levels within the same signal-responsive cell. SYS-1 binds to the conserved N-terminal β-catenin-binding domain (CBD) of POP-1 and functions as a transcriptional co-activator. Phosphorylation of POP-1 by LIT-1, the C. elegans Nemo-like kinase homolog, promotes POP-1 nuclear export and is the main mechanism by which POP-1 nuclear levels are lowered. We present a mechanism whereby SYS-1 and POP-1 nuclear levels are regulated in opposite directions, despite the fact that the two proteins physically interact. We show that the C terminus of POP-1 is essential for LIT-1 phosphorylation and is specifically bound by the diverged β-catenin WRM-1. WRM-1 does not bind to the CBD of POP-1, nor does SYS-1 bind to the C-terminal domain. Furthermore, binding of WRM-1 to the POP-1 C terminus is mutually inhibitory with SYS-1 binding at the CBD. Computer modeling provides a structural explanation for the specificity in WRM-1 and SYS-1 binding to POP-1. Finally, WRM-1 exhibits two independent and distinct molecular functions that are novel for β-catenins: WRM-1 serves both as the substrate-binding subunit and an obligate regulatory subunit for the LIT-1 kinase. Mutual inhibitory binding would result in two populations of POP-1: one bound by WRM-1 that is LIT-1 phosphorylated and exported from the nucleus, and another, bound by SYS-1, that remains in the nucleus and transcriptionally activates Wnt target genes. These studies could provide novel insights into cancers arising from aberrant Wnt activation.

Indexed as

Gene Expression Regulation, DevelopmentalAmino Acid SequenceAnimalsbeta CateninBody PatterningCaenorhabditis elegansCaenorhabditis elegans ProteinsCell NucleusCytoskeletal ProteinsDNA-Binding ProteinsGreen Fluorescent ProteinsHeLa CellsHigh Mobility Group ProteinsHumansMembrane ProteinsModels, Biologicalbeta CateninCaenorhabditis elegans ProteinsCytoskeletal ProteinsDNA-Binding ProteinsGreen Fluorescent ProteinsHigh Mobility Group Proteinslit-1 protein, C elegansMembrane Proteinspop-1 protein, C elegansProtein Serine-Threonine KinasesSys-1 protein, C elegansTranscription FactorsWRM-1 protein, C elegans

Identifiers

PMID21852394
PMCPMC3171225
OpenAlexW1980350000

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.