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P is a modular protein with intrinsically disordered regions and folded domains that plays specific and similar roles in the replication of the different viruses and, in some cases, hijacks cell components to the advantage of the virus and is involved in immune evasion. All P proteins are multimeric, but the role of this multimerization is still unclear. Here, we demonstrate that the dimerization domain of VSV P is dispensable for the expression of virally encoded proteins and for virus growth in cell culture. This provides new insights into and raises questions about the functioning of the RNA-synthesizing machinery of the nonsegmented negative-sense RNA viruses.<\/jats:p>","DOI":"10.1128\/jvi.01789-19","type":"journal-article","created":{"date-parts":[[2019,12,13]],"date-time":"2019-12-13T10:51:43Z","timestamp":1576234303000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":10,"title":["Vesicular Stomatitis Virus Phosphoprotein Dimerization Domain Is Dispensable for Virus Growth"],"prefix":"10.1128","volume":"94","author":[{"given":"Francine C. 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