Scaffold-mediated phosphatase regulation in EGFR family signaling

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ID: 332854
2026
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Abstract
Abstract The epidermal growth factor receptor (EGFR) family serves as an archetypal model of receptor tyrosine kinase signaling and plays essential roles in development, tissue homeostasis, and cancer. Although receptor phosphorylation has been extensively studied, the mechanisms governing dephosphorylation remain comparatively obscured. A limited repertoire of protein tyrosine phosphatases (PTPs) directly regulates EGFR family receptors, yet their signaling specificity cannot be explained by intrinsic catalytic activity alone. Accumulating evidence indicates that PTP function is governed by higher-order mechanisms that control subcellular localization, receptor accessibility, and integration into dynamic signaling networks. In this Review, we summarize the PTPs that directly regulate the EGFR family and examine how scaffold proteins, membrane organization, intracellular trafficking, and organelle-specific platforms coordinate receptor dephosphorylation. We propose a functional taxonomy comprising five categories: assembly, localization, membrane-organizing, organelle, and regulatory scaffolds. This framework provides a basis for understanding signaling specificity and suggests therapeutic strategies targeting the spatiotemporal organization of phosphatase function.
Reference Key
openalex_W7222918641 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Shigeki Higashiyama, Eilma Akter-Yasuoka, Hiroyuki Takeda, Jun Nakayama
Journal The Journal of Biochemistry
Year 2026
DOI
10.1093/jb/mvag075
URL
https://doi.org/10.1093/jb/mvag075
Keywords Keywords not found

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