{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T20:15:11Z","timestamp":1789848911774,"version":"4.0.1"},"reference-count":36,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2011,12,5]],"date-time":"2011-12-05T00:00:00Z","timestamp":1323043200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Intl Journal of Cancer"],"published-print":{"date-parts":[[2012,9]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Infection of erythroid cells by Friend spleen focus\u2010forming virus (SFFV) leads to acute erythroid hyperplasia in mice, due to expression of its unique envelope glycoprotein, gp55. Erythroid cells expressing SFFV gp55 proliferate in the absence of their normal regulator, erythropoietin, because of the interaction among the viral envelope protein, the erythropoietin receptor, and a short form of the receptor tyrosine kinase Stk (sf\u2010Stk). This leads to constitutive activation of several signal transduction pathways. Our previous studies showed that sf\u2010Stk interacts with SFFV gp55, forming disulfide\u2010linked complexes. This covalent interaction, along with other noncovalent interactions with SFFV\u2010gp55, results in constitutive tyrosine phosphorylation of sf\u2010Stk and rodent fibroblast transformation. Here, we determined the precise amino acid region within sf\u2010Stk that contributes to fibroblast transformation by the polycythemia\u2010inducing (SFFV\u2010P) and the anemia\u2010inducing (SFFV\u2010A) strains of SFFV. Sf\u2010Stk deletion mutants showed different transforming abilities in fibroblasts infected with SFFV\u2010P and SFFV\u2010A, although the N\u2010terminal extracellular domain of sf\u2010Stk was essential for fibroblast transformation by both viruses. Point mutations of sf\u2010Stk indicated that cysteine 19 was critical for fibroblast transformation by SFFV\u2010P, although all four cysteines (8, 19, 37 and 42) appeared to be important for fibroblast transformation by both SFFV\u2010P and SFFV\u2010A. Mutation of sf\u2010Stk cysteine 19 abolished its ability to form dimers with SFFV\u2010P and SFFV\u2010A gp55. These results suggest that the interaction between sf\u2010Stk and the envelope proteins of the polycythemia\u2010 and anemia\u2010inducing variants of SFFV is architecturally different.<\/jats:p>","DOI":"10.1002\/ijc.27330","type":"journal-article","created":{"date-parts":[[2011,10,27]],"date-time":"2011-10-27T11:55:15Z","timestamp":1319716515000},"page":"1083-1094","source":"Crossref","is-referenced-by-count":4,"title":["Role of N\u2010terminal sequences of the tyrosine kinase sf\u2010Stk in transformation of rodent fibroblasts by variants of Friend spleen focus\u2010forming virus"],"prefix":"10.1002","volume":"131","author":[{"given":"Daigo","family":"Umehara","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maki","family":"Kawamura","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuka","family":"Odahara","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shinya","family":"Watanabe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charlotte","family":"Hanson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sandra","family":"Ruscetti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kazuo","family":"Nishigaki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2011,12,5]]},"reference":[{"key":"e_1_2_5_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1357-2725(99)00074-6"},{"key":"e_1_2_5_3_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.2990034"},{"key":"e_1_2_5_4_2","first-page":"163","article-title":"Fv\u20102: 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