About: NEDD4 family ubiquitin ligases associate with LCMV Z’s PPXY domain and are required for virus budding, but not via direct ubiquitination of Z

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About: NEDD4 family ubiquitin ligases associate with LCMV Z’s PPXY domain and are required for virus budding, but not via direct ubiquitination of Z Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	NEDD4 family ubiquitin ligases associate with LCMV Z’s PPXY domain and are required for virus budding, but not via direct ubiquitination of Z
Creator	Eisenhauer, Philip King, Benjamin Id, David Klaus, Joseph Botten Id, Jason Dang Id, Loan Id, Bryan Id, Emily Id, Jamie Manuelyan Id, Inessa Mattice Id, Ethan Weir Id, Marion Ziegler Id, Christopher
source	PMC
abstract	Viral late domains are used by many viruses to recruit the cellular endosomal sorting complex required for transport (ESCRT) to mediate membrane scission during viral budding. Unlike the P(S/T)AP and YPX((1–3))L late domains, which interact directly with the ESCRT proteins Tsg101 and ALIX, the molecular linkage connecting the PPXY late domain to ESCRT proteins is unclear. The mammarenavirus lymphocytic choriomeningitis virus (LCMV) matrix protein, Z, contains only one late domain, PPXY. We previously found that this domain in LCMV Z, as well as the ESCRT pathway, are required for the release of defective interfering (DI) particles but not infectious virus. To better understand the molecular mechanism of ESCRT recruitment by the PPXY late domain, affinity purification-mass spectrometry was used to identify host proteins that interact with the Z proteins of the Old World mammarenaviruses LCMV and Lassa virus. Several Nedd4 family E3 ubiquitin ligases interact with these matrix proteins and in the case of LCMV Z, the interaction was PPXY-dependent. We demonstrated that these ligases directly ubiquitinate LCMV Z and mapped the specific lysine residues modified. A recombinant LCMV containing a Z that cannot be ubiquitinated maintained its ability to produce both infectious virus and DI particles, suggesting that direct ubiquitination of LCMV Z alone is insufficient for recruiting ESCRT proteins to mediate virus release. However, Nedd4 ligases appear to be important for DI particle release suggesting that ubiquitination of targets other than the Z protein itself is required for efficient viral ESCRT recruitment.
has issue date	2019-11-11(xsd:dateTime)
bibo:doi	10.1371/journal.ppat.1008100
bibo:pmid	31710650
has license	cc-by
sha1sum (hex)	687da34d9c50dd79ad55b5067ffdbb7282c03d35
schema:url	https://doi.org/10.1371/journal.ppat.1008100
resource representing a document's title	NEDD4 family ubiquitin ligases associate with LCMV Z’s PPXY domain and are required for virus budding, but not via direct ubiquitination of Z
has PubMed Central identifier	PMC6874086
has PubMed identifier	31710650
schema:publication	PLoS Pathog
resource representing a document's body	covid:687da34d9c50dd79ad55b5067ffdbb7282c03d35#body_text
is schema:about of	named entity 'Nedd4' named entity 'particles' named entity 'viral budding' named entity 'linkage' covid:arg/687da34d9c50dd79ad55b5067ffdbb7282c03d35 named entity 'connecting' named entity 'However' named entity 'membrane' named entity 'molecular' named entity 'family' named entity 'late' named entity 'ESCRT' named entity 'lymphocytic choriomeningitis virus' named entity 'late' named entity 'ubiquitination' named entity 'identify' named entity 'late' named entity 'proteins' named entity 'matrix' named entity 'lysine' named entity 'family' named entity 'ESCRT' named entity 'affinity purification-mass spectrometry' named entity 'ESCRT' named entity 'virus' named entity 'E3 ubiquitin ligases' named entity 'molecular mechanism' named entity 'YPX' named entity 'ubiquitination' named entity 'ESCRT' named entity 'ubiquitinated' named entity 'LCMV' named entity 'virus budding' named entity 'ubiquitination' named entity 'NEDD4' named entity 'ESCRT' named entity 'virus' named entity 'LCMV' named entity 'Spastin' named entity 'plasmids' named entity 'conservative substitution' named entity 'autophagy' named entity 'ESCRT' named entity 'endocytosis' named entity 'lysed' named entity 'biogenesis' named entity 'peptides' named entity 'ESCRT-III' named entity 'siRNAs' named entity '0.01' named entity 'interactomes' named entity 'ubiquitin' named entity 'transfection' named entity 'Nedd4' named entity 'Nedd4' named entity 'ubiquitination' named entity 'YPX' named entity 'C-terminal' named entity 'Nedd4' named entity 'lysine' named entity 'ubiquitin' named entity 'threonine' named entity 'ESCRT' named entity 'ubiquitinated protein' named entity 'affinity purification' named entity 'ESCRT' named entity 'Nedd4' named entity 'lysines' named entity 'Protein'

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