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Adv."],"published-print":{"date-parts":[[2026,7,24]]},"abstract":"<jats:p>Endocytosis is central to cellular trafficking and signaling across eukaryotes, yet whether and how plant viruses actively reprogram this pathway remains unclear. Here, we show that the geminiviral betasatellite\u2013encoded \u03b2C1 reprograms the host VPS9a-Rab5 endocytic module to promote viral infection. \u03b2C1 associates with the Rab5 GTPases ARA6 and ARA7 as well as their guanine nucleotide exchange factor VPS9a, stabilizing the VPS9a-Rab5 complex and enhancing nucleotide exchange. This catalytic potentiation sustains Rab5 activation and drives endosome proliferation, which, in turn, stabilizes \u03b2C1 to support efficient viral replication. Genetic disruption of Rab5 or VPS9a compromises endocytosis, reduces \u03b2C1 accumulation, and restricts infection by multiple geminiviruses. Together, these findings define the VPS9a-Rab5 module as a central proviral hub linking host membrane dynamics to effector stability and viral DNA amplification, revealing an unanticipated strategy in which a viral effector amplifies a cellular regulatory catalyst to reprogram a fundamental cellular pathway for virus infection.<\/jats:p>","DOI":"10.1126\/sciadv.aeg2304","type":"journal-article","created":{"date-parts":[[2026,7,24]],"date-time":"2026-07-24T17:58:33Z","timestamp":1784915913000},"update-policy":"https:\/\/doi.org\/10.34133\/aaas_crossmark","source":"Crossref","is-referenced-by-count":1,"title":["A viral protein diverts the endocytic VPS9a-Rab5 pathway to promote virus infection in plants"],"prefix":"10.1126","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5445-7004","authenticated-orcid":true,"given":"Tuxunaili","family":"Aizitili","sequence":"first","affiliation":[{"name":"College of Life Sciences, Shihezi University, Shihezi 832003, 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