| Literature DB >> 29634939 |
Dean J Procter1, Avik Banerjee2, Masatoshi Nukui3, Kevin Kruse4, Vadim Gaponenko5, Eain A Murphy3, Yulia Komarova4, Derek Walsh6.
Abstract
Human cytomegalovirus (HCMV), a leading cause of congenital birth defects, forms an unusual cytoplasmic virion maturation site termed the "assembly compartment" (AC). Here, we show that the AC also acts as a microtubule-organizing center (MTOC) wherein centrosome activity is suppressed and Golgi-based microtubule (MT) nucleation is enhanced. This involved viral manipulation of discrete functions of MT plus-end-binding (EB) proteins. In particular, EB3, but not EB1 or EB2, was recruited to the AC and was required to nucleate MTs that were rapidly acetylated. EB3-regulated acetylated MTs were necessary for nuclear rotation prior to cell migration, maintenance of AC structure, and optimal virus replication. Independently, a myristoylated peptide that blocked EB3-mediated enrichment of MT regulatory proteins at Golgi regions of the AC also suppressed acetylated MT formation, nuclear rotation, and infection. Thus, HCMV offers new insights into the regulation and functions of Golgi-derived MTs and the therapeutic potential of targeting EB3.Entities:
Keywords: Golgi; acetylation; cell migration; cytomegalovirus; end-binding protein; microtubule organizing center; nuclear rotation; virus infection
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Year: 2018 PMID: 29634939 PMCID: PMC5896778 DOI: 10.1016/j.devcel.2018.03.010
Source DB: PubMed Journal: Dev Cell ISSN: 1534-5807 Impact factor: 12.270