Evidence map›Paper›PMID 42475177›Full record

ArticleCell reports2026

AXL phosphosite mapping links FAK1 and YAP1 signaling to erlotinib resistance in EGFR-mutant lung cancer.

Marc Creixell, Scott D Taylor, Jacqueline Gerritsen, Mingxuan Jiang, Song Yi Bae, Teresa Augustin, Michelle Loui, Carmen Boixo, Saki Minamino, Victoria Gong and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

13 authors.

Marc CreixellDepartment of Bioengineering, University of California, Los Angeles, Los Angeles, CA 90095, USA; Jonsson Comprehensive Cancer Center, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Scott D TaylorDepartment of Bioengineering, University of California, Los Angeles, Los Angeles, CA 90095, USA; Jonsson Comprehensive Cancer Center, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Jacqueline GerritsenDepartment of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Center for Precision Cancer Medicine, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Mingxuan JiangCancer Research UK Cambridge Institute, University of Cambridge, Li Ka Shing Centre, Robinson Way, Cambridge CB2 2RE, UK.
Song Yi BaeDepartment of Bioengineering, University of California, Los Angeles, Los Angeles, CA 90095, USA; Jonsson Comprehensive Cancer Center, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Teresa AugustinCancer Research UK Cambridge Institute, University of Cambridge, Li Ka Shing Centre, Robinson Way, Cambridge CB2 2RE, UK.
Michelle LouiDepartment of Bioengineering, University of California, Los Angeles, Los Angeles, CA 90095, USA; Jonsson Comprehensive Cancer Center, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Carmen BoixoDepartment of Bioengineering, University of California, Los Angeles, Los Angeles, CA 90095, USA; Jonsson Comprehensive Cancer Center, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Saki MinaminoDepartment of Bioengineering, University of California, Los Angeles, Los Angeles, CA 90095, USA; Jonsson Comprehensive Cancer Center, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Victoria GongDepartment of Bioengineering, University of California, Los Angeles, Los Angeles, CA 90095, USA; Jonsson Comprehensive Cancer Center, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Pau CreixellCancer Research UK Cambridge Institute, University of Cambridge, Li Ka Shing Centre, Robinson Way, Cambridge CB2 2RE, UK.
Forest M WhiteDepartment of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA; Center for Precision Cancer Medicine, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Aaron S MeyerDepartment of Bioengineering, University of California, Los Angeles, Los Angeles, CA 90095, USA; Jonsson Comprehensive Cancer Center, University of California, Los Angeles, Los Angeles, CA 90095, USA. Electronic address: ameyer@g.ucla.edu.

Funding

Precision lung cancer therapy design through multiplexed adapter measurementU01CA215709 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HAURA, ERIC B., MEYER, AARON SAMUEL · 2017 to 2021
$2.3M
NCI NIH HHS U01 CA215709
6 · The paper itself

Abstract

Targeted therapies for receptor tyrosine kinases are effective but invariably limited by drug resistance. In EGFR-mutant lung cancer, AXL activation drives resistance to erlotinib by restoring cell survival and migration. To map these signaling mechanisms, we generated a panel of lung adenocarcinoma PC9 cell lines with phenylalanine substitutions at each intracellular AXL tyrosine residue. By integrating phosphorylation data with phenotypic changes via multivariate modeling, we found that AXL signaling organizes into two clusters enriched for Abl1 and SFK substrate motifs. A peptide specificity screen identified FAK1 as a top proximal substrate of AXL. Downstream, AXL-mediated YAP1 activation was found to sustain drug tolerance, while combined inhibition eliminated persister cells in vitro. These AXL and YAP pathways correlate with disease progression and poor clinical outcomes in erlotinib-treated patients. Collectively, this study dissects the specific signaling regulators by which AXL drives erlotinib resistance.

Indexed as

Adaptor Proteins, Signal TransducingDrug Resistance, NeoplasmErlotinib HydrochlorideFocal Adhesion Kinase 1Lung NeoplasmsMutationPhosphoproteinsProto-Oncogene ProteinsReceptor Protein-Tyrosine KinasesTranscription FactorsAxl Receptor Tyrosine KinaseCell Line, TumorErbB ReceptorsHumansPhosphorylationSignal TransductionAdaptor Proteins, Signal TransducingAXL protein, humanAxl Receptor Tyrosine KinaseEGFR protein, humanErbB ReceptorsErlotinib HydrochlorideFocal Adhesion Kinase 1PhosphoproteinsProto-Oncogene ProteinsReceptor Protein-Tyrosine KinasesTranscription FactorsYAP1 protein, humanYAP-Signaling ProteinsAXLcomputational modelingCP: cancerdrug resistanceEGFRkinase biologyLUADsystems biology

Identifiers

PMID42475177
PMCPMC13480988

What OpenQuestion holds

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Registered trials

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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.