{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T01:42:51Z","timestamp":1791164571286,"version":"4.1.0"},"reference-count":48,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2002,3,19]],"date-time":"2002-03-19T00:00:00Z","timestamp":1016496000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Genes Chromosomes &amp;amp; Cancer"],"published-print":{"date-parts":[[2002,7]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The <jats:italic>SSX<\/jats:italic> gene family is composed of at least five functional and highly homologous members, <jats:italic>SSX1<\/jats:italic> to <jats:italic>SSX5,<\/jats:italic> that are normally expressed in only the testis and thyroid. <jats:italic>SSX1,<\/jats:italic> <jats:italic>SSX2,<\/jats:italic> or <jats:italic>SSX4<\/jats:italic> may be fused to the <jats:italic>SYT<\/jats:italic> gene as a result of the t(X;18) translocation in synovial sarcoma. In addition, the <jats:italic>SSX1, SSX2, SSX4,<\/jats:italic> and <jats:italic>SSX5<\/jats:italic> genes were found to be aberrantly expressed in several other malignancies, including melanoma. The SSX proteins are localized in the nucleus and are diffusely distributed. In addition, they may be included in polycomb\u2010group nuclear bodies. Other studies have indicated that the SSX proteins may act as transcriptional repressors. As a first step toward the elucidation of the cellular signaling networks in which the SSX proteins may act, we used the yeast two\u2010hybrid system to identify SSX2\u2010interacting proteins. By doing so, two novel human proteins were detected: RAB3IP, the human homolog of an interactor of the Ras\u2010like GTPase Rab3A; and a novel protein, SSX2IP. RAB3IP did not interact with either SSX1, SSX3, or SSX4 in the yeast two\u2010hybrid system, whereas SSX2IP interacted with SSX3 but not with either SSX1 or SSX4. Further analysis of deletion mutants showed that both RAB3IP and SSX2IP interact with the N\u2010terminal moiety of the SSX2 protein. Immunofluorescence analyses of transfected cells revealed that the RAB3IP protein is normally localized in the cytoplasm. However, coexpression of both RAB3IP and SSX2 led to colocalization of both proteins in the nucleus. Likewise, the SSX2IP protein was found to be colocalizing with SSX2 in the nucleus. By performing glutathione\u2010<jats:italic>S<\/jats:italic>\u2010transferase pull\u2010down assays, we found that both RAB3IP and SSX2IP interact directly with SSX2 in vitro. These newly observed protein\/protein interactions may have important implications for the mechanisms underlying normal and malignant cellular growth. \u00a9 2002 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/gcc.10073","type":"journal-article","created":{"date-parts":[[2002,8,25]],"date-time":"2002-08-25T23:27:00Z","timestamp":1030318020000},"page":"285-298","source":"Crossref","is-referenced-by-count":50,"title":["The cancer\u2010related protein SSX2 interacts with the human homologue of a Ras\u2010like GTPase interactor, RAB3IP, and a novel nuclear protein, SSX2IP"],"prefix":"10.1002","volume":"34","author":[{"given":"Diederik R.H.","family":"de Bruijn","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nuno R.","family":"dos 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