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• W2387303566 abstract "The assembly of retroviruses is decepand this signals int tively simple. Only the product of the tosis. The enzymol gag gene is required for the formation of gation is complex. a virus-like particle (1). After its synthesis tion of ubiquitin in the cytoplasm Gag is targeted to the enzyme called El, plasma membrane, where Gag-Gag interof ubiquitin to El actions, Gag-RNA interactions, Gagester bond. The ub membrane interactions, and perhaps GagE1 to a second er host protein interactions lead to a bulging zyme, E3, which m out of the nascent virus particle, first as a E2, then transfers horseshoe-shaped and then as a lollipopgroups of the tar shaped structure that can be visualized by cells have only or electron microscopy. The process of memdozens of differer brane envelopment of the virus is called which confer spec budding. The last step in budding is a ubiquitination. ir membrane fusion event that serves to different ubiquitin pinch off the virus, releasing it into the cleave the isopept medium. Late in assembly, perhaps conubiquitins or betcomitant with pinching off or just precedtarget protein (11 ing it, a viral protease cleaves Gag at Despite lack of several sites, leading to a morphological larity, the Gag pr change in the virus. This process is called different genera maturation and is essential for the virus tostructurally simi structurally simil; become infectious.common domains In this issue of PNAS, three articles by roteins uon roi independent groups provide an important MA (matrix) doi new clue to the mechanism by which retm roviruses bud from the plasma membrane merae taret (2-4). The articles implicate the cellular mate vof t pmar ' / 1. ... . , .i ..i tface of the memb protein ubiquitin in a late step in budding. Ubiquitin is a small highly conserved domain partpate 76-aa protein well known for its role in form s th e core she protein degradation by the proteasome The NC ucleo (5). In proteins targeted for degradation, Te N (nucleoc ubiquitin becomes coupled via its Cnize the packagin terminal glycine residue to the e-amino RNA, and the ma group of lysine residues in the protein (or deses the RNA I rarely to the N-terminal a-amino group), the three commor forming an isopeptide bond. Other ubiqproteins have othe uitin proteins are similarly coupled to whose functions h lysine residues in this first ubiquitin, and cidated and which thus the target protein ends up carrying a era. Deletion ana ramified polyubiquitin chain that acts as aavian Rous sarcon signal recognized by the proteasome (6). as well as a few ott By mechanisms that are incompletely unshown that much c derstood, the targeted protein is degraded budding, when bu while the ubiquitin molecules are recymally as the efficie cled. A less well-known role for ubiquitin enveloped and pa is in endocytosis of plasma membrane medium. The seg: proteins (7, 8). For example, this process essential are called has been studied with yeast plasma memto be confused w brane receptors (9) and with human separated by clean growth hormone receptor (10). In yeast a These essential se~ single ubiquitin moiety becomes coupled sequence called th' to the cytoplasmic tail of the receptor in is required for ef response to stimulation of the receptor, the virus bud (12-: mbly: Actor or bystander?" @default.
• W2387303566 created "2016-06-24" @default.
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• W2387303566 date "2016-01-01" @default.
• W2387303566 modified "2023-09-23" @default.
• W2387303566 title "Ubiquitin in retrovirus ass" @default.
• W2387303566 hasPublicationYear "2016" @default.
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