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EGFR\u2013SHC1 fusion protein comprises of N-terminal EGFR and C-terminal SHC1. We demonstrated that EGFR\u2013SHC1 simultaneously activates the EGFR kinase domain (KD) and SRC-mediated phosphorylation of the SHC1 fusion partner, thereby driving ERK\/AKT pathway activation and tumorigenesis independent of KD inhibition. Structural modeling coupled with domain-specific mutagenesis revealed that SHC1 phosphorylation establishes a kinase-independent bypass mechanism. Notably, dual-targeted inhibition using afatinib (EGFR-TKI) in combination with dasatinib (SRC-TKI) induced marked tumor regression in a TKI-refractory patient with NSCLC with EGFR\u2013SHC1. This study illustrates a cooperative oncogenesis between kinases and scaffold proteins in fusions, providing a clinically actionable strategy for overcoming TKI resistance in patients with these oncogenic fusions.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Significance:<\/jats:title>\n                    <jats:p>This study identifies a previously unrecognized mode of oncogenic signaling in receptor tyrosine kinase (RTK) fusions, in which a non-kinase fusion partner actively drives tumorigenesis through kinase-independent mechanisms. By challenging the classical kinase-centric model of RTK fusions, it provides a framework for understanding intrinsic resistance to TKIs and for developing rational combination therapies.<\/jats:p>\n                    <jats:p>See related commentary by Le and Wolf, p. 1480<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1158\/2159-8290.cd-25-1936","type":"journal-article","created":{"date-parts":[[2026,3,24]],"date-time":"2026-03-24T15:26:18Z","timestamp":1774365978000},"page":"1573-1589","update-policy":"https:\/\/doi.org\/10.1158\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["The Oncogenic\n                    <i>EGFR\u2013SHC1<\/i>\n                    Fusion Confers Insensitivity to EGFR-TKIs via Dual Activation of N-EGFR Kinase Domain and C-SHC1 Phosphorylation Sites in Lung 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