Evidence map›Paper›PMID 41326667›Full record

ArticleCommunications biology2025

KSR1 is a scaffold for the Hippo signaling pathway.

Samar Sayedyahossein, Mohammed Rizwan Babu Sait, Zhigang Li, Riddhi Banerjee, Andy Tran, Louise Thines, Mehdi Karimi, Mehrnoosh Bahmani, Naomi Mishan, Pooya Borzou and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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

12 authors.

Samar SayedyahosseinDepartment of Laboratory Medicine, National Institutes of Health, Bethesda, MD, USA. samaryahossein@vtc.vt.edu.ORCID http://orcid.org/0000-0003-1773-4740
Mohammed Rizwan Babu SaitDepartment of Laboratory Medicine, National Institutes of Health, Bethesda, MD, USA.
Zhigang LiDepartment of Laboratory Medicine, National Institutes of Health, Bethesda, MD, USA.
Riddhi BanerjeeDepartment of Laboratory Medicine, National Institutes of Health, Bethesda, MD, USA.
Andy TranConfocal Microscopy Core Facility, Laboratory of Cancer Biology and Genetics, NCI, National Institutes of Health, Bethesda, MD, USA.ORCID http://orcid.org/0000-0002-2388-7121
Louise ThinesDepartment of Laboratory Medicine, National Institutes of Health, Bethesda, MD, USA.
Mehdi KarimiDepartment of Mathematics, Illinois State University, Normal, IL, USA.
Mehrnoosh BahmaniDepartment of Physics and Chemistry, Illinois State University, Normal, IL, USA.
Naomi MishanDepartment of Physiology and Pharmacology, University of Western Ontario, London, ON, Canada.
Pooya BorzouDepartment of Electrical and Computer Engineering, Isfahan University of Technology, Isfahan, Iran.
Sergio A HassanBioinformatics and Computational Biosciences Branch, OCICB, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health, Bethesda, MD, USA.
David B SacksDepartment of Laboratory Medicine, National Institutes of Health, Bethesda, MD, USA. sacksdb@mail.nih.gov.ORCID http://orcid.org/0000-0003-3100-0735

Funding

U.S. Department of Health & Human Services | National Institutes of Health (NIH) Intramural research program
6 · The paper itself

Abstract

The evolutionarily conserved Hippo signaling pathway regulates organ size and tissue homeostasis. Yes-associated protein (YAP) functions as a transcriptional co-activator and is a critical downstream effector of the Hippo signaling pathway. Altered crosstalk with oncogenic signaling pathways contributes to YAP dysregulation in cancer. Kinase Suppressor of Ras 1 (KSR1) scaffolds the Ras cascade. Some of the functions of the Ras and Hippo pathways in regulating cellular processes are similar. Nevertheless, the potential intersection of Ras and Hippo signaling has not been explored. Here, we identify KSR1 as a previously unrecognized scaffold of the Hippo pathway. We demonstrate that KSR1 constitutively binds to YAP and MST1 and forms a complex with LATS1. Moreover, KSR1 modulates YAP protein levels and its transcriptional activity, at least in part through the RhoA/actin axis. Our findings provide insight into the role of KSR1 as a scaffold of the Hippo signaling that could yield novel therapeutics.

Indexed as

Adaptor Proteins, Signal TransducingProtein KinasesProtein Serine-Threonine KinasesSignal TransductionCell Cycle ProteinsHEK293 CellsHippo Signaling PathwayHumansPhosphoproteinsrhoA GTP-Binding ProteinTranscription FactorsYAP-Signaling ProteinsAdaptor Proteins, Signal TransducingCell Cycle ProteinsKSR-1 protein kinaseLATS1 protein, humanPhosphoproteinsProtein KinasesProtein Serine-Threonine KinasesrhoA GTP-Binding ProteinRHOA protein, humanTranscription FactorsYAP1 protein, humanYAP-Signaling Proteins

Identifiers

PMID41326667
PMCPMC12669712

What Socratic holds

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LicenceCC BY
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 Socratic graph.