Nascent G signal peptide is cleaved at ER membrane

Stable Identifier
R-HSA-9830882
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 G signal peptide is cleaved at ER membrane
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The leading 65 amino acids of nascent membrane-bound G protein variant of RSV, assumed to be the signal sequence directing it to the endoplasmic reticulum (ER) membrane, are cleaved off by an unknown enzyme (Fernie et al, 1985; Ding et al, 1987). 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 membrane-bound G protein signal peptidase.
Literature References
PubMed ID Title Journal Year
4031826 Kinetics of synthesis of respiratory syncytial virus glycoproteins

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

J Gen Virol 1985
3113070 Expression and glycosylation of the respiratory syncytial virus G protein in Saccharomyces cerevisiae

Ding, MX, Wen, DZ, Schlesinger, MJ, Wertz, GW, Ball, LA

Virology 1987
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  (2023-03-15)
Reviewed
Bergeron, HC  (2023-11-03)
Created
Stephan, R  (2023-03-16)
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