A tandem recruitment site in the pseudokinase scaffold PEAK3 is subject to phosphorylation-dependent regulation and cancer-associated mutations.

Tianyue Zhao, Jianmei Hou, Changyuan Hu, Thomas R Cotton, Roger J Daly

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

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Tianyue ZhaoCancer Program, Biomedicine Discovery Institute, Monash University, Melbourne, VIC, Australia; Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, Australia.

Jianmei HouCancer Program, Biomedicine Discovery Institute, Monash University, Melbourne, VIC, Australia; Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, Australia; Laura and Isaac Perlmutter Cancer Center, New York University Grossman School of Medicine, NYU Langone Health, New York, New York, USA.

Changyuan HuCancer Program, Biomedicine Discovery Institute, Monash University, Melbourne, VIC, Australia; Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, Australia; Wenzhou Medical University-Monash BDI Alliance in Clinical and Experimental Biomedicine, the First Affiliated Hospital of Wenzhou Medical University, Wenzhou, China.

Thomas R CottonCancer Program, Biomedicine Discovery Institute, Monash University, Melbourne, VIC, Australia; Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, Australia.

Roger J DalyCancer Program, Biomedicine Discovery Institute, Monash University, Melbourne, VIC, Australia; Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, Australia. Electronic address: roger.daly@monash.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The PEAK protein family, comprising PEAK1-3, are pseudokinase scaffolds that regulate cell proliferation and motility via recruitment of specific effectors. For PEAK3, the latter include the adaptor proteins Grb2 and CrkII and the Arf GTPase-activating protein (ArfGAP) ASAP1. PEAK3 exhibits a tandem site spanning a CrkII SH3 domain binding sequence and phosphorylation-dependent 14-3-3 recruitment motif at serine 69 (S69), with 14-3-3 binding mediating a negative control 'switch' on PEAK3 signaling. However, whether this control switch is subject to (patho)physiological regulation has remained unclear. Here, using MCF-10A breast epithelial cells as a model system, we demonstrate that S69 phosphorylation occurs predominantly in the cytoplasm and is subject to growth factor regulation, being enhanced by EGF and insulin stimulation but with distinct temporal dynamics. We identify Ca

Indexed as

Adaptor Proteins, Signal TransducingMutationNeoplasmsEpidermal Growth FactorGRB2 Adaptor ProteinHumansPhosphorylationAdaptor Proteins, Signal TransducingEpidermal Growth FactorGRB2 Adaptor Proteincell signalingprotein-protein interactionserine/threonine phosphorylationsignal transduction

Identifiers

PMID41819264

DOI10.1016/j.jbc.2026.111365

PMCPMC13089168

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LicenceCC BY-NC-ND

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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.