Evidence map›Paper›PMID 28373297›Full record

ArticleMolecular & cellular proteomics : MCP2017

Regulation of Protein Interactions by

Shawn Xiong, Amber L Couzens, Michelle J Kean, Daniel Y Mao, Sebastian Guettler, Igor Kurinov, Anne-Claude Gingras, Frank Sicheri

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
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  15. The HIPPO pathway in gynecological malignancies.American journal of cancer research · 2020
    Review
  16. Article
  17. Review
  18. Polarity in Ciliate Models: From Cilia to Cell Architecture.Frontiers in cell and developmental biology · 2019
    Review
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  20. 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 5 institutions in 3 countries.

Shawn XiongFrom the ‡Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada, M5G 1X5.
Amber L CouzensFrom the ‡Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada, M5G 1X5.ORCID 0000-0003-0057-6686
Michelle J KeanFrom the ‡Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada, M5G 1X5.
Daniel Y MaoFrom the ‡Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada, M5G 1X5.
Sebastian GuettlerFrom the ‡Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada, M5G 1X5.
Igor Kurinov‖NE-CAT APS, Building 436E, Argonne National Lab, 9700 S. Cass Avenue, Argonne, Illinois 60439.
Anne-Claude GingrasFrom the ‡Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada, M5G 1X5; gingras@lunenfeld.ca sicheri@lunenfeld.ca.ORCID 0000-0002-6090-4437
Frank SicheriFrom the ‡Lunenfeld-Tanenbaum Research Institute, Sinai Health System, Toronto, Ontario, Canada, M5G 1X5; gingras@lunenfeld.ca sicheri@lunenfeld.ca.
Sinai Health System · CAArgonne National Laboratory · USInstitute of Cancer Research · GBLunenfeld-Tanenbaum Research Institute · CAUniversity of Toronto · CA

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
CIHR FDN 143277CIHR FDN 143301NCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403
6 · The paper itself

Abstract

MOB1 is a multifunctional protein best characterized for its integrative role in regulating Hippo and NDR pathway signaling in metazoans and the Mitotic Exit Network in yeast. Human MOB1 binds both the upstream kinases MST1 and MST2 and the downstream AGC group kinases LATS1, LATS2, NDR1, and NDR2. Binding of MOB1 to MST1 and MST2 is mediated by its phosphopeptide-binding infrastructure, the specificity of which matches the phosphorylation consensus of MST1 and MST2. On the other hand, binding of MOB1 to the LATS and NDR kinases is mediated by a distinct interaction surface on MOB1. By assembling both upstream and downstream kinases into a single complex, MOB1 facilitates the activation of the latter by the former through a trans-phosphorylation event. Binding of MOB1 to its upstream partners also renders MOB1 a substrate, which serves to differentially regulate its two protein interaction activities (at least

Indexed as

Adaptor Proteins, Signal TransducingHippo KinasesIntracellular Signaling Peptides and ProteinsPhosphoprotein PhosphatasesPhosphorylationProtein Serine-Threonine KinasesProteomicsRho Guanine Nucleotide Exchange FactorsSerine-Threonine Kinase 3Adaptor Proteins, Signal TransducingHippo KinasesIntracellular Signaling Peptides and ProteinsLATS1 protein, humanMOB1B protein, humanPhosphoprotein Phosphatasesprotein phosphatase-6 SAPSP1 subunit, humanProtein Serine-Threonine KinasesRho Guanine Nucleotide Exchange FactorsSerine-Threonine Kinase 3STK38 protein, humanSTK3 protein, humanSTK4 protein, human

Identifiers

PMID28373297
PMCPMC5461541
OpenAlexW2604182146

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.