About: The C-terminal domain of the MERS coronavirus M protein contains a trans-Golgi network localization signal

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About: The C-terminal domain of the MERS coronavirus M protein contains a trans-Golgi network localization signal Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The C-terminal domain of the MERS coronavirus M protein contains a trans-Golgi network localization signal
Creator	Dubuisson, Jean Rouillé, Yves Goffard, Anne Danneels, Adeline Desmarets, Lowiese Belouzard, X Bonnin, Ariane Perrier, Anabelle
Source	Medline; PMC
abstract	Coronavirus M proteins represent the major protein component of the viral envelope. They play an essential role during viral assembly by interacting with all of the other structural proteins. Coronaviruses bud into the endoplasmic reticulum (ER)–Golgi intermediate compartment (ERGIC), but the mechanisms by which M proteins are transported from their site of synthesis, the ER, to the budding site remain poorly understood. Here, we investigated the intracellular trafficking of the Middle East respiratory syndrome coronavirus (MERS-CoV) M protein. Subcellular localization analyses revealed that the MERS-CoV M protein is retained intracellularly in the trans-Golgi network (TGN), and we identified two motifs in the distal part of the C-terminal domain as being important for this specific localization. We identified the first motif as a functional diacidic DxE ER export signal, because substituting Asp-211 and Glu-213 with alanine induced retention of the MERS-CoV M in the ER. The second motif, (199)KxGxYR(204), was responsible for retaining the M protein in the TGN. Substitution of this motif resulted in MERS-CoV M leakage toward the plasma membrane. We further confirmed the role of (199)KxGxYR(204) as a TGN retention signal by using chimeras between MERS-CoV M and the M protein of infectious bronchitis virus (IBV). Our results indicated that the C-terminal domains of both proteins determine their specific localization, namely TGN and ERGIC/cis-Golgi for MERS-M and IBV-M, respectively. Our findings indicate that MERS-CoV M protein localizes to the TGN because of the combined presence of an ER export signal and a TGN retention motif.
has issue date	2019-08-09(xsd:dateTime)
bibo:doi	10.1074/jbc.ra119.008964
bibo:pmid	31399512
has license	bronze-oa
sha1sum (hex)	35c9282c1b7a5918691efe6f35ca60111bfd590c
schema:url	https://doi.org/10.1074/jbc.ra119.008964
resource representing a document's title	The C-terminal domain of the MERS coronavirus M protein contains a trans-Golgi network localization signal
has PubMed Central identifier	PMC6768645
has PubMed identifier	31399512
schema:publication	Journal of Biological Chemistry
resource representing a document's body	covid:35c9282c1b7a5918691efe6f35ca60111bfd590c#body_text
is schema:about of	named entity 'viral' named entity 'viral envelope' named entity 'C-terminal domain' covid:arg/35c9282c1b7a5918691efe6f35ca60111bfd590c named entity 'They' named entity 'bud' named entity 'Golgi intermediate compartment' named entity 'trans-Golgi network' named entity 'mutation' named entity 'biotin' named entity 'IBV' named entity 'antibodies' named entity 'protein' named entity 'N-glycosylation site' named entity 'biotin' named entity 'Tyr' named entity 'motif' named entity 'streptavidin' named entity 'EcoRI' named entity 'assay' named entity 'protein' named entity 'COPI' named entity 'goat' named entity 'IgG' named entity 'nonpermeable' named entity 'mutation' named entity 'plasma membrane' named entity 'protein' named entity 'VSVG' named entity 'incubation' named entity 'GTPase' named entity 'cyanine' named entity 'colocalization' named entity 'sheep' named entity 'HCoV-NL63' named entity 'protein' named entity 'Pearson correlation coefficient' named entity 'primary antibodies' named entity 'glycosylation' named entity 'intracellular retention' named entity 'motif' named entity 'porcine epidemic diarrhea virus' named entity 'mutation' named entity 'mutation' named entity 'PCC' named entity 'confocal microscopy' named entity 'protein' named entity 'protein' named entity 'mutation' named entity 'ER-Golgi intermediate compartment' named entity 'motif' named entity 'mutation' named entity 'M protein' named entity 'protein' named entity 'subcellular localization' named entity 'mutation' named entity 'IBV' named entity 'TGN' named entity 'protein' named entity 'biotinylation' named entity 'coatomer' named entity 'motif' named entity 'protein' named entity 'MERS-CoV' named entity 'glycosyltransferases' named entity 'immunoblotting' named entity 'subcellular localization' named entity 'mutation' named entity 'TGN' named entity 'mutation' named entity 'Multimeric' named entity 'Sec23' named entity 'PCC' named entity 'transmembrane domain'

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