Reactome | Recruitment of Spike trimer to assembling virion

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Recruitment of Spike trimer to assembling virion Show undefined attributes

authored	[InstanceEdit:9685154] Rothfels, Karen, 2020-04-22
category	binding
compartment	[Compartment:6791047] endoplasmic reticulum-Golgi intermediate compartment membrane
created	[InstanceEdit:9684240] Rothfels, Karen, 2020-04-21
crossReference	[DatabaseIdentifier:12020764] Mondo:0005091
dbId	9684241
disease	[Disease:9678120] severe acute respiratory syndrome
displayName	Recruitment of Spike trimer to assembling virion
edited	[InstanceEdit:9685483] Rothfels, Karen, 2020-04-23
eventOf	[Pathway:R-HSA-9679509] Virion Assembly and Release - Homo sapiens
followingEvent	[Reaction:R-HSA-9686174] Accessory proteins are recruited to the maturing virion - Homo sapiens
input	75 × [Complex:R-COV-9683768] complex N-glycan-PALM-Spike trimer [endoplasmic reticulum-Golgi intermediate compartment] [Complex:R-COV-9684226] M lattice:E protein:encapsidated SARS coronavirus genomic RNA [endoplasmic reticulum-Golgi intermediate compartment membrane]
isChimeric	false
isInDisease	true
isInferred	false
literatureReference	[LiteratureReference:9685450] Incorporation of spike and membrane glycoproteins into coronavirus virions [LiteratureReference:9685465] A single tyrosine in the severe acute respiratory syndrome coronavirus membrane protein cytoplasmic tail is important for efficient interaction with spike protein [LiteratureReference:9685364] Interactions between M protein and other structural proteins of severe, acute respiratory syndrome-associated coronavirus [LiteratureReference:9685466] Two palmitylated cysteine residues of the severe acute respiratory syndrome coronavirus spike (S) protein are critical for S incorporation into virus-like particles, but not for M-S co-localization [LiteratureReference:9682993] Palmitoylation of SARS-CoV S protein is necessary for partitioning into detergent-resistant membranes and cell-cell fusion but not interaction with M protein [LiteratureReference:9684005] Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy [LiteratureReference:9683990] The SARS coronavirus nucleocapsid protein--forms and functions [LiteratureReference:9686429] The cytoplasmic tail of the severe acute respiratory syndrome coronavirus spike protein contains a novel endoplasmic reticulum retrieval signal that binds COPI and promotes interaction with membrane protein [LiteratureReference:9686427] The contribution of the cytoplasmic retrieval signal of severe acute respiratory syndrome coronavirus to intracellular accumulation of S proteins and incorporation of S protein into virus-like particles
maxDepth	1
modified	[InstanceEdit:9830342] Matthews, Lisa, 2023-03-08
name	Recruitment of Spike trimer to assembling virion
orthologousEvent	[Reaction:R-HSA-9694553] Recruitment of Spike trimer to assembling virion - Homo sapiens
output	[Complex:R-COV-9686310] S3:M:E:encapsidated SARS coronavirus genomic RNA:O-glycosyl 3a tetramer [endoplasmic reticulum-Golgi intermediate compartment membrane]
precedingEvent	[Reaction:R-HSA-9684238] E and N are recruited to the M lattice - Homo sapiens [BlackBoxEvent:R-HSA-9683648] Spike trimer glycoside chains are extended - Homo sapiens
relatedSpecies	[Species:9678119] Human SARS coronavirus
releaseDate	2020-06-10
reviewStatus	[ReviewStatus:9821382] five stars
reviewed	[InstanceEdit:9690206] Acencio, Marcio Luis, Mazein, Alexander, 2020-05-27
schemaClass	Reaction
species	[Species:48887] Homo sapiens
stId	R-HSA-9684241
summation	[Summation:9685494] S trimers are recruited to the assembling virion through int...
updateTrackers	[UpdateTracker:9776672] Update Tracker - [Reaction:9684241] Recruitment of Spike trimer to assembling virion - v74:[modifyText]

Referrals

(updatedInstance)	[UpdateTracker:9776672] Update Tracker - [Reaction:9684241] Recruitment of Spike trimer to assembling virion - v74:[modifyText]
(hasEvent)	[Pathway:R-HSA-9679509] Virion Assembly and Release
(precedingEvent)	[Reaction:R-HSA-9686174] Accessory proteins are recruited to the maturing virion

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