Nascent F signal peptide is cleaved at ER membrane

Stable Identifier
R-HSA-9829030
Type
Reaction [uncertain]
Species
Homo sapiens
Related Species
Human respiratory syncytial virus A
Compartment
cytosol, endoplasmic reticulum membrane
ReviewStatus
5/5
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Nascent F signal peptide is cleaved at ER membrane
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Human respiratory syncytial virus (hRSV) A protein F moves to the endoplasmic reticulum (ER) membrane co-translationally, which is accompanied by the cleavage of its signal peptide and release of the transmembrane fusion protein precursor (Fernie et al, 1985; Brock et al, 2005). While the responsible peptidase has not been experimentally investigated, signal peptides of human proteins are cleaved by the signal peptidase complex (SPC) located at the endoplasmic reticulum membrane. This complex, which can exist in two versions, SPC-A and SPC-C, that differ in their catalytic subunits (SEC11A in SPC-A, and SEC11C in SPC-C), is known to be involved in cleavage of signal peptides in other viruses (Liaci et al. 2021), and is a plausible candidate for the nascent F protein signal peptidase.
Literature References
PubMed ID Title Journal Year
16160180 The transmembrane domain of the respiratory syncytial virus F protein is an orientation-independent apical plasma membrane sorting sequence

Brock, SC, Heck, JM, McGraw, PA, Crowe, JE

J Virol 2005
4031826 Kinetics of synthesis of respiratory syncytial virus glycoproteins

Fernie, BF, Dapolito, G, Cote, PJ, Gerin, JL

J Gen Virol 1985
Participants
Input
Output
Participates
as an event of
Catalyst Activity

serine-type endopeptidase activity of (Signal Peptidase Complex) [endoplasmic reticulum membrane]

Physical Entity
(Signal Peptidase Complex) [endoplasmic reticulum membrane] (Homo sapiens)
Activity
serine-type endopeptidase activity (GO:0004252)
Disease
Cross References
Mondo
Authored
Stephan, R  (2023-02-18)
Reviewed
Bergeron, HC  (2023-11-03)
Created
Stephan, R  (2023-02-22)
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