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Mounting evidence suggests that, in addition to recognizing phosphorylated tyrosine (pTyr) residues through specific phosphobinding modules, many protein kinases selectively recognize pTyr directly adjacent to the tyrosine residue they phosphorylate and catalyze the formation of twin pTyr-pTyr sites. Here, we demonstrate the importance of this phosphopriming-driven twin pTyr signaling in promoting cell cycle progression through the cell cycle-inhibitory protein p27\n                  <jats:sup>Kip1<\/jats:sup>\n                  . We identify, structurally resolve, and tune two distinct molecular determinants driving the selective recognition of pTyr directly N- and C-terminal to the target phospho-acceptor tyrosine site. We further show structural and biochemical conservation in this recognition, and identify cancer-associated alterations to these determinants that are unable to recognize phosphoprimed substrates. Finally, using an\n                  <jats:italic>in vivo<\/jats:italic>\n                  mouse model of leukemia we show that Bcr-Abl mutants unable to recognize phosphoprimed substrates paradoxically result in enhanced tumor development and progression. These data indicate that Bcr-Abl, like other proto-oncogenes such as Ras or Myc, engages both pro- and anti-oncogenic programs \u2013 but in the case of Bcr-Abl, this is accomplished through a mechanism involving traditional and phosphoprimed substrate recognition.\n                <\/jats:p>","DOI":"10.1101\/2025.06.10.658871","type":"posted-content","created":{"date-parts":[[2025,6,11]],"date-time":"2025-06-11T18:30:11Z","timestamp":1749666611000},"source":"Crossref","is-referenced-by-count":2,"title":["Structural Identification of Major Molecular Determinants for Phosphotyrosine Recognition in Tyrosine Kinases Reveals Tumour Promoting and Suppressive Functions"],"prefix":"10.64898","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2614-8682","authenticated-orcid":false,"given":"Nuo","family":"Cheng","sequence":"first","affiliation":[{"name":"Cancer Research UK Cambridge Institute, University of Cambridge, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luis 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