Affinage

PEAK1

Inactive tyrosine-protein kinase PEAK1 · UniProt Q9H792

Length
1746 aa
Mass
193.1 kDa
Annotated
2026-06-10
38 papers in source corpus 19 papers cited in narrative 19 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PEAK1 is a pseudokinase scaffold that localizes to focal adhesions and the actin cytoskeleton, where it acts as a phosphorylation-regulated assembly platform integrating signals from receptor tyrosine kinases, Src-family kinases, and integrins to control cell migration, adhesion dynamics, and epithelial-mesenchymal transition (PMID:23105102, PMID:35687021). Its pseudokinase domain adopts a closed nucleotide-binding cleft and is flanked by N- and C-terminal helical extensions that form a split-helical dimerization (SHED) region, enabling PEAK1 self-association and heterodimerization with the related pseudokinase SgK223; this dimerization is required for full signaling output to Grb2/Stat3 and for efficient migration (PMID:29212708, PMID:27531744). PEAK1 function is gated by Src-family phosphorylation: phosphorylation at Tyr-665 governs proper focal-adhesion localization and the kinetics of adhesion assembly/disassembly, while Lyn/Src phosphorylation of Tyr-635 creates a docking site that recruits Grb2 to drive Stat3 and ERK activation and recruits the Tensin3 SH2 domain to couple PEAK1 to RGD-binding integrins (PMID:23105102, PMID:23378338, PMID:35687021). Additional phosphosites extend its interactome — pY1188 recruits Shc1 to link PEAK1 to EGFR signaling, and Src-dependent pY724 promotes binding to ZO-1, masking its LC3-interacting region to protect tight junctions from autophagic degradation (PMID:35687021, PMID:40707483). PEAK1 reciprocally activates Src through CSK binding and assembles adhesion-remodeling complexes such as the AXL–NEDD9–CRKII–PEAK1–CSK module that phosphorylates Paxillin to drive focal-adhesion disassembly and invasion (PMID:32681075, PMID:40707483). Through these activities PEAK1 promotes oncogenic signaling and metastasis across multiple tumor contexts, including a CAMK2–PEAK1–PEAK2 feed-forward loop in triple-negative breast cancer and switching of TGFβ signaling toward non-canonical Src/MAPK and ZEB1-driven EMT (PMID:26267863, PMID:39984440). In intestinal epithelium, PEAK1 loss in vivo reduces Src activity and ZO-1 levels, disrupting tight junctions and increasing intestinal permeability (PMID:40707483).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2012 High

    Established that PEAK1 is a focal-adhesion and actin-cytoskeleton protein whose function depends on dynamic Src-family phosphorylation, defining it as a spatiotemporally regulated adhesion scaffold rather than a static structural component.

    Evidence PEAK1 knockdown, Y665F and phosphomimetic mutagenesis, live-cell focal adhesion imaging, and Src inhibition in migrating cells

    PMID:23105102

    Open questions at the time
    • Did not identify the direct partners recruited to pY665
    • Mechanism linking phosphorylation to adhesion turnover kinetics unresolved
  2. 2012 Medium

    Placed PEAK1 within an oncogenic KRas-driven Src/ErbB2 amplification loop, linking it to receptor-tyrosine-kinase-inhibitor resistance in pancreatic cancer.

    Evidence In vivo tumor models with RNAi knockdown and pathway epistasis between Src, PEAK1, and ErbB2

    PMID:22589274

    Open questions at the time
    • Direct biochemical interactions among the loop components not mapped
    • Single-lab in vivo epistasis
  3. 2013 High

    Identified Tyr-635 as a major Lyn/Src phosphosite that functions as a Grb2-docking site coupling PEAK1 to Stat3 and ERK activation, providing the first defined molecular output of PEAK1 phosphorylation.

    Evidence Lyn substrate phosphoproteomics, Co-IP, Y635F mutagenesis, and 3D culture invasion assays

    PMID:23378338

    Open questions at the time
    • Whether Grb2 recruitment is direct to pY635 versus bridged not fully resolved
    • Quantitative contribution of Stat3 vs ERK arms not separated
  4. 2014 Medium

    Showed PEAK1 expression is controlled by hypusinated eIF5A, positioning PEAK1 as a translationally regulated effector in pancreatic cancer growth.

    Evidence eIF5A knockdown/overexpression, DHPS/DOHH inhibitors, and orthotopic tumor models with PEAK1 Western blot

    PMID:25261239

    Open questions at the time
    • Direct vs indirect regulation of PEAK1 translation not distinguished
    • Single lab
  5. 2015 Medium

    Defined PEAK1 as a switch that reroutes TGFβ signaling from canonical Smad2/3 to non-canonical Src/MAPK and ZEB1-driven EMT in a fibronectin/integrin context.

    Evidence PEAK1 knockdown/overexpression, pathway reporter assays, fibronectin/ITGB3 manipulation, ZEB1 analysis, and in vivo metastasis models

    PMID:26267863 PMID:26297948

    Open questions at the time
    • Molecular basis of the Smad-to-Src/MAPK switch unresolved
    • Single-lab findings
  6. 2016 High

    Demonstrated that PEAK1 homo- and heterodimerizes with SgK223 via CH and PK domains, and that SgK223 is required for full PEAK1 signaling output, establishing dimerization as a determinant of scaffold activity.

    Evidence Mass spectrometry interactomics, pulldowns, size-exclusion chromatography, CRISPR SgK223 knockout, and migration/Stat3 assays

    PMID:27531744

    Open questions at the time
    • Stoichiometry and architecture of the heterodimer not structurally defined
    • How dimerization gates downstream signaling mechanistically unclear
  7. 2017 High

    Provided the structural basis for PEAK1 as a pseudokinase, showing a closed nucleotide-binding cleft and a SHED dimerization region conserved with pragmin/SgK223.

    Evidence X-ray crystallography of the PEAK1 pseudokinase domain at 2.3 Å with sequence conservation analysis

    PMID:29212708

    Open questions at the time
    • Full-length structure including N-terminal regulatory regions not determined
    • Whether any nucleotide or small molecule can engage the cleft unknown
  8. 2018 Medium

    Connected PEAK1 to ERK1/2 and JAK2 activation driving EMT and metastasis, and to a PPP1R12B complex modulating Grb2/PI3K/Akt signaling, broadening its downstream pathway repertoire across cancer types.

    Evidence PEAK1 KO/OE, Co-IP with PPP1R12B, pharmacologic ERK/JAK2/PI3K-Akt inhibition, and in vivo metastasis models

    PMID:30038287 PMID:30472186

    Open questions at the time
    • Direct vs indirect engagement of JAK2 and PI3K not established
    • Single-lab studies in distinct tumor contexts
  9. 2020 High

    Resolved a defined adhesion-remodeling module in which AXL-phosphorylated NEDD9 recruits CRKII to PEAK1, which complexes with CSK to drive Paxillin phosphorylation and focal-adhesion disassembly, mechanistically linking PEAK1 to invasion downstream of AXL.

    Evidence Phosphoproteomics, Co-IP, proximity labeling, RNAi, and in vivo metastasis assays

    PMID:32681075

    Open questions at the time
    • Direct kinase responsible for Paxillin phosphorylation within the complex not pinned down
    • Temporal ordering of complex assembly unresolved
  10. 2021 Medium

    Extended the PEAK1 interactome to ALK in neuroblastoma and to stromal/transcriptional regulation, showing ALK-activity-dependent interaction, SNAI2-driven PEAK1 expression in MSCs promoting INHBA-mediated lapatinib resistance, and CDC5L-driven PEAK1 transcription activating ERK1/2 and JAK2.

    Evidence BioID/LC-MS with lorlatinib validation; MSC co-culture with PEAK1 KD and INHBA neutralization; ChIP and luciferase reporter assays

    PMID:32167655 PMID:34239043 PMID:34273398

    Open questions at the time
    • Functional consequence of the ALK–PEAK1 interaction not defined
    • Direct vs indirect transcriptional control by CDC5L and SNAI2 not fully separated
  11. 2022 High

    Mapped how PEAK1 physically couples to adhesion machinery, showing Tensin3-SH2 binding to pY635 bridges PEAK1 to RGD-binding integrins and pY1188 recruits Shc1, defining phosphosite-specific integrin and EGFR linkages.

    Evidence BioID of β1/β3 integrins, Co-IP, and mutagenesis of Y635, Y1188, and the integrin NPxY motif with migration assays

    PMID:35687021

    Open questions at the time
    • How simultaneous use of distinct phosphosites is coordinated unresolved
    • Direct structural model of the Tensin3–PEAK1–integrin assembly absent
  12. 2024 Medium

    Tested PEAK1 requirement in genetic CRC models, finding it dispensable for Apc/Kras/Pten-driven tumor formation in vivo despite promoting EGF-induced proliferation and spheroid polarization in vitro, refining its in vivo context-dependence.

    Evidence CRISPR PEAK1 knockout in Apc/Kras/Pten CRC mouse models, in vitro proliferation, and 3D spheroid assays

    PMID:39532961

    Open questions at the time
    • Why in vitro signaling roles do not translate to in vivo tumor dependence unexplained
    • Possible compensation by paralogs not addressed
  13. 2025 High

    Established new mechanistic axes: a CAMK2D/G–PEAK1–PEAK2 feed-forward loop via PLCγ1/Ca2+ in TNBC, and a Src-pY724-dependent PEAK1–ZO-1 interaction that masks ZO-1's LIR to protect tight junctions from autophagy, with PEAK1 loss disrupting intestinal barrier integrity in vivo.

    Evidence AP-MS, Co-IP, domain mapping (aa 714–731), Y724 mutagenesis, CAMK2 inhibitor RA306, autophagy assays, and PEAK1 conditional KO mice with colitis models

    PMID:39984440 PMID:40707483

    Open questions at the time
    • Structural basis of PEAK1–PEAK2 association via CAMK2 phosphorylation not determined
    • How ZO-1 protective and oncogenic functions of PEAK1 are integrated unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved how PEAK1's many phosphosite-specific interactions, dimerization states, and tissue-specific roles are integrated into a unified regulatory logic, and whether its pseudokinase fold has any catalytic-independent allosteric activity.
  • No full-length structure capturing regulatory regions and dimer interfaces
  • No unifying model of how competing partners are selected at distinct phosphosites
  • RHOV–PEAK1 axis rests on a single preprint without reconstitution

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 6 GO:0098772 molecular function regulator activity 3
Localization
GO:0005829 cytosol 2 GO:0005856 cytoskeleton 1
Pathway
R-HSA-162582 Signal Transduction 4 R-HSA-1643685 Disease 4 R-HSA-1474244 Extracellular matrix organization 3
Partners
CAMK2DCRKIICSKGRB2SGK223SHC1TNS3ZO-1
Complex memberships
AXL-NEDD9-CRKII-PEAK1-CSK complexPEAK1-PEAK2 complexPEAK1-SgK223 heterodimer

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2017 X-ray crystal structure of the PEAK1 pseudokinase domain (2.3 Å resolution) revealed a closed nucleotide-binding cleft that may preclude nucleotide binding, and identified N- and C-terminal extensions forming an all α-helical split-helical dimerization (SHED) region that mediates dimerization conserved between PEAK1 and pragmin (SgK223). X-ray crystallography, sequence conservation analysis The Journal of biological chemistry High 29212708
2012 PEAK1 localizes to the actin cytoskeleton and focal adhesions in migrating cells; phosphorylation of Tyr-665 (by Src family kinases) is required for normal PEAK1 localization and regulation of focal adhesion assembly and disassembly kinetics; constitutive phosphorylation at Tyr-665 is also disruptive, indicating a requirement for dynamic, spatiotemporally precise regulation. PEAK1 knockdown, phospho-site mutagenesis (Y665F and phosphomimetic), live-cell focal adhesion imaging, Src inhibitor treatment The Journal of biological chemistry High 23105102
2012 Oncogenic KRas induces a kinase amplification loop involving Src, PEAK1, and ErbB2 in pancreatic cancer cells; blockade of ErbB2 increased Src-dependent PEAK1 expression and PEAK1-dependent Src activation, suggesting PEAK1 mediates ErbB2-inhibitor resistance. In vivo tumor models, RNAi knockdown, pathway epistasis Cancer research Medium 22589274
2013 The Src family kinase Lyn directly phosphorylates PEAK1 (SgK269) in basal breast cancer cells; Tyr-635 is a major Lyn phosphorylation site on PEAK1 and serves as a Grb2-binding site that promotes Stat3 and Erk activation; mutation Y635F abrogates enhanced acinar size and cellular invasion. Phosphoproteomics (Lyn substrate identification), Co-IP, Y635F mutagenesis, 3D culture invasion assays, RNAi Cancer research High 23378338
2016 PEAK1 (SgK269) undergoes homotypic self-association and heterotypic association with the related pseudokinase SgK223; both associations require the CH (coiled-helix) and PK (pseudokinase) domains of both proteins; SgK269 bridges SgK223 to Grb2 but cannot activate Stat3 or efficiently enhance migration in SgK223 knockout cells, demonstrating that SgK223 is required for full SgK269 signaling output. Mass spectrometry-based interactomics, pulldowns, size-exclusion chromatography, CRISPR/Cas9 SgK223 KO, migration and Stat3 activation assays The Journal of biological chemistry High 27531744
2020 AXL phosphorylates NEDD9, leading to NEDD9 binding to CRKII, which in turn associates with PEAK1; PEAK1 forms a complex with the tyrosine kinase CSK to mediate phosphorylation of PAXILLIN, thereby driving focal adhesion disassembly, cell migration and invasion downstream of AXL. Phosphoproteomics, Co-IP, proximity labeling, RNAi knockdown, in vivo metastasis assays Nature communications High 32681075
2022 PEAK1 interacts indirectly with RGD-binding integrins (α5β1, αVβ3, αVβ5) in focal adhesions through Tensin3; the SH2 domain of Tensin3 binds phosphorylated Tyr-635 on PEAK1 (phosphorylated by Src), and both the integrin β-tail NPxY motif and PEAK1 pY635 are required for this interaction; additionally, phosphorylated Tyr-1188 on PEAK1 recruits Shc1 to focal adhesions, linking PEAK1 to late EGFR/Shc1 signaling. BioID proximity labeling of β1/β3 integrins, Co-IP, mutagenesis (Y635, NPxY), cell migration assays The Journal of cell biology High 35687021
2015 PEAK1 mediates signaling cross talk between TGFβ receptors and integrin/Src/MAPK pathways; in the context of fibronectin, high PEAK1 expression switches TGFβ signaling from canonical Smad2/3 to non-canonical Src and MAPK pathways, promoting EMT, proliferation and metastasis; PEAK1 is necessary for TGFβ to induce ZEB1-mediated EMT. PEAK1 knockdown/overexpression, Smad2/3 and Src/MAPK pathway reporter assays, fibronectin/ITGB3 manipulation, in vivo metastasis models PloS one Medium 26267863
2015 PEAK1 is necessary for TGFβ-induced ZEB1 expression and ZEB1-mediated EMT in oncogene-transformed mammary epithelial cells and triple-negative breast cancer cells, specifically in the context of fibronectin/ITGB3 activation. RNAi knockdown, fibronectin/integrin β3 manipulation, ZEB1 Western blot, EMT marker analysis Biochemical and biophysical research communications Medium 26297948
2014 eIF5A proteins regulate PDAC cell growth by modulating PEAK1 expression; hypusination of eIF5A (catalyzed by DHPS and DOHH) is required for this regulation, and pharmacologic inhibition of eIF5A hypusination suppresses PEAK1 levels and PDAC cell growth. eIF5A knockdown/overexpression, DHPS/DOHH inhibitors, orthotopic tumor models, Western blot for PEAK1 Cancer research Medium 25261239
2021 PEAK1 is identified by BioID as a component of the ALK proximitome in neuroblastoma cells; PEAK1 was validated as an ALK interactor in NB cells; interaction was dependent on ALK kinase activity (blocked by lorlatinib). BioID proximity labeling, LC/MS-MS, validation Co-IP/pulldown with ALK TKI lorlatinib Journal of molecular biology Medium 34273398
2025 PEAK1 interacts with ZO-1 via a conserved region (amino acids 714–731), masking the LC3-interacting region on ZO-1 and preventing autophagy-mediated ZO-1 degradation; Src-mediated phosphorylation of PEAK1 at Y724 promotes the PEAK1–ZO-1 interaction; PEAK1 also binds CSK to positively regulate Src activity; loss of PEAK1 in intestinal epithelial cells reduces Src activity and ZO-1 levels, disrupting tight junctions and increasing intestinal permeability in vivo. Co-IP, mutagenesis (Y724), domain mapping (aa 714–731), autophagy assays, PEAK1 conditional KO mice, colitis models Nature communications High 40707483
2025 PEAK1 promotes CAMK2D and CAMK2G activation in TNBC cells via PLCγ1/Ca2+ signaling and direct binding to CAMK2 through a consensus CAMK2 interaction motif in the PEAK1 N-terminus; in turn, CAMK2 phosphorylates PEAK1 to enhance its association with PEAK2, which is critical for PEAK1 oncogenic signaling. Affinity purification-mass spectrometry, Co-IP, CAMK2 inhibitor (RA306), CRISPR PEAK1 ablation, TNBC xenograft/metastasis models Nature communications High 39984440
2021 In HER2-positive breast cancer, PEAK1 in mesenchymal stem cells (MSCs) mediates secretion of INHBA/activin-A, which promotes lapatinib resistance in co-cultured breast cancer cells; SNAI2 is an upstream transcriptional regulator of PEAK1 in stromal cells. MSC-tumor cell co-culture, PEAK1 knockdown in MSCs, conditioned media experiments, single-cell CycIF, INHBA neutralization Oncogene Medium 34239043
2021 CDC5L protein binds directly to the PEAK1 gene promoter to promote PEAK1 transcription in ovarian cancer cells; PEAK1 overexpression in turn activates ERK1/2 and JAK2 signaling pathways. Chromatin immunoprecipitation (ChIP), luciferase reporter assay, Western blot for ERK1/2 and JAK2 phosphorylation Cancer medicine Medium 32167655
2018 PEAK1 promotes lung cancer EMT and metastasis by enhancing activation of ERK1/2 and JAK2 signaling pathways; combined inhibition of ERK1/2 (PD98059) and JAK2 (AZD1480) reverses PEAK1-induced EMT, migration and invasion. PEAK1 overexpression/KO, Western blot for p-ERK1/2 and p-JAK2, pharmacologic inhibitors, in vivo metastasis model Cell death & disease Medium 30038287
2018 PEAK1 forms a complex with PPP1R12B (protein phosphatase 1 regulatory subunit 12B) in colorectal cancer cells; this axis suppresses activation of the Grb2/PI3K/Akt pathway; PI3K/Akt inhibitors reverse the effects of PEAK1 loss on cell proliferation, migration and invasion. Co-IP, PPP1R12B KD/OE, PI3K/Akt inhibitors, in vitro and in vivo tumor models Cancer letters Medium 30472186
2025 RHOV (an atypical Rho GTPase) directly interacts with PEAK1 as identified by immunoprecipitation coupled with LC-MS; the RHOV-PEAK1 complex is required for MYC upregulation and PI3K/MAPK signaling in NSCLC; PEAK1 depletion abolishes RHOV-driven MYC upregulation; additionally, PEAK1 maintains RHOV expression by inhibiting TGF-β signaling, establishing a negative feedback loop. Co-IP/LC-MS, PEAK1 and RHOV siRNA knockdown, Western blot for MYC/PI3K/MAPK, RNA-seq bioRxivpreprint Low bio_10.1101_2025.04.18.649622
2024 PEAK1 ablation in CRC mouse models driven by Apc loss (with or without oncogenic Kras or Pten loss) does not significantly contribute to tumor formation in vivo, although PEAK1 promotes EGF-induced Caco-2 cell proliferation and regulates spheroid polarization/lumenization in vitro. CRISPR/Cas9 PEAK1 KO, in vivo CRC mouse models (Apc, Kras, Pten), in vitro proliferation assays, 3D spheroid culture Scientific reports Medium 39532961

Source papers

Stage 0 corpus · 38 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2012 KRas induces a Src/PEAK1/ErbB2 kinase amplification loop that drives metastatic growth and therapy resistance in pancreatic cancer. Cancer research 96 22589274
2014 A hypusine-eIF5A-PEAK1 switch regulates the pathogenesis of pancreatic cancer. Cancer research 86 25261239
2013 Involvement of Lyn and the atypical kinase SgK269/PEAK1 in a basal breast cancer signaling pathway. Cancer research 79 23378338
2020 AXL confers cell migration and invasion by hijacking a PEAK1-regulated focal adhesion protein network. Nature communications 55 32681075
2018 PEAK1, acting as a tumor promoter in colorectal cancer, is regulated by the EGFR/KRas signaling axis and miR-181d. Cell death & disease 50 29449544
2018 The PEAK1-PPP1R12B axis inhibits tumor growth and metastasis by regulating Grb2/PI3K/Akt signalling in colorectal cancer. Cancer letters 49 30472186
2018 Overexpression of PEAK1 contributes to epithelial-mesenchymal transition and tumor metastasis in lung cancer through modulating ERK1/2 and JAK2 signaling. Cell death & disease 45 30038287
2015 PEAK1 Acts as a Molecular Switch to Regulate Context-Dependent TGFβ Responses in Breast Cancer. PloS one 45 26267863
2017 The crystal structure of pseudokinase PEAK1 (Sugen kinase 269) reveals an unusual catalytic cleft and a novel mode of kinase fold dimerization. The Journal of biological chemistry 40 29212708
2020 Circ-PGAM1 promotes malignant progression of epithelial ovarian cancer through regulation of the miR-542-3p/CDC5L/PEAK1 pathway. Cancer medicine 37 32167655
2015 Identification of a PEAK1/ZEB1 signaling axis during TGFβ/fibronectin-induced EMT in breast cancer. Biochemical and biophysical research communications 37 26297948
2012 Dynamic phosphorylation of tyrosine 665 in pseudopodium-enriched atypical kinase 1 (PEAK1) is essential for the regulation of cell migration and focal adhesion turnover. The Journal of biological chemistry 35 23105102
2016 Homo- and Heterotypic Association Regulates Signaling by the SgK269/PEAK1 and SgK223 Pseudokinases. The Journal of biological chemistry 27 27531744
2021 A SNAI2-PEAK1-INHBA stromal axis drives progression and lapatinib resistance in HER2-positive breast cancer by supporting subpopulations of tumor cells positive for antiapoptotic and stress signaling markers. Oncogene 26 34239043
2021 LncRNA NORAD, sponging miR-363-3p, promotes invasion and EMT by upregulating PEAK1 and activating the ERK signaling pathway in NSCLC cells. Journal of bioenergetics and biomembranes 18 33742335
2022 PEAK1 Y635 phosphorylation regulates cell migration through association with Tensin3 and integrins. The Journal of cell biology 17 35687021
2021 Importance of Circ0009910 in colorectal cancer pathogenesis as a possible regulator of miR-145 and PEAK1. World journal of surgical oncology 15 34479583
2014 Analysis of a cytoskeleton-associated kinase PEAK1 and E-cadherin in gastric cancer. Pathology, research and practice 14 25445115
2022 Potential therapeutic effects of hAMSCs secretome on Panc1 pancreatic cancer cells through downregulation of SgK269, E-cadherin, vimentin, and snail expression. Biologicals : journal of the International Association of Biological Standardization 13 35216916
2017 The pseudokinases SgK269 and SgK223: A novel oncogenic alliance in human cancer. Cell adhesion & migration 12 29105536
2025 PEAK1 maintains tight junctions in intestinal epithelial cells and resists colitis by inhibiting autophagy-mediated ZO-1 degradation. Nature communications 10 40707483
2021 BioID-Screening Identifies PEAK1 and SHP2 as Components of the ALK Proximitome in Neuroblastoma Cells. Journal of molecular biology 10 34273398
2021 PEAK1 promotes invasion and metastasis and confers drug resistance in breast cancer. Clinical and experimental medicine 10 34554318
2021 Pseudopodium enriched atypical kinase 1(PEAK1) promotes invasion and of melanoma cells by activating JAK/STAT3 signals. Bioengineered 8 34365903
2022 Exosome-delivered circSATB2 targets the miR-330-5p/PEAK1 axis to regulate proliferation, migration and invasion of lung cancer cells. Thoracic cancer 7 36148757
2016 Ascending the PEAK1 toward targeting TGFβ during cancer progression: Recent advances and future perspectives. Cancer cell & microenvironment 6 29392163
2025 Activation of CAMK2 by pseudokinase PEAK1 represents a targetable pathway in triple negative breast cancer. Nature communications 5 39984440
2025 Self-calibrated SERS-LFIA biosensor based on AgNF for in-site and rapid detection of protein kinase biomarker PEAK1. Biosensors & bioelectronics 4 40716336
2023 LncRNA-PEAK1 promotes neuronal apoptosis after intracerebral hemorrhage by miR-466i-5p/caspase 8 axis. Heliyon 4 37095973
2023 Evaluation of SgK269 expression in colon cancer patients and the effects of hAMSCs secretome on tumor invasion through SgK269/c-Src/p-P130Cas/p-Paxillin/p-ERK1/2 signaling pathway in HT-29 colon cancer cells. 3 Biotech 4 37744286
2024 Targeting PEAK1 sensitizes anaplastic thyroid carcinoma cells harboring BRAFV600E to Vemurafenib by Bim upregulation. Histology and histopathology 3 38284248
2025 Black Phosphorus-Loaded Gelatin Methacryloyl Hydrogels Enhance Angiogenesis via Activation of the PEAK1-MAPK Pathway. ACS applied materials & interfaces 2 40272250
2026 PEAK1 promotes prostate cancer progression and docetaxel resistance by mediating the polarization of tumor-associated macrophages. European journal of medical research 1 41495812
2024 Feed-forward stimulation of CAMK2 by the oncogenic pseudokinase PEAK1 generates a therapeutically "actionable" signalling axis in triple negative breast cancer. bioRxiv : the preprint server for biology 1 38405732
2024 MicroRNA-505-3p mediates cell motility of epithelial ovarian cancer via suppressing PEAK1 expression. Journal of biochemical and molecular toxicology 1 39003575
2025 The expression of circSATB2, PEAK1 in non-small cell lung cancer tissue and their relationships with clinical pathological characteristics, as well as postoperative recurrence and metastasis. General physiology and biophysics 0 40326976
2025 CRISPR/Cas13a-mediated interfacial cleaving of hairpin RNA reporter for PEAK1 nucleic acid sensing. RSC advances 0 41048551
2024 Colorectal carcinoma progression is not influenced by the pseudokinase PEAK1. Scientific reports 0 39532961

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