Reactome | Human respiratory syncytial virus (hRSV) A protein F moves t...

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created	[InstanceEdit:9829041] Stephan, Ralf, 2023-02-22
dbId	9829045
displayName	Human respiratory syncytial virus (hRSV) A protein F moves t...
literatureReference	[LiteratureReference:9829036] Kinetics of synthesis of respiratory syncytial virus glycoproteins [LiteratureReference:9829067] The transmembrane domain of the respiratory syncytial virus F protein is an orientation-independent apical plasma membrane sorting sequence [LiteratureReference:9833168] Structure of the human signal peptidase complex reveals the determinants for signal peptide cleavage
modified	[InstanceEdit:9833183] Orlic-Milacic, Marija, 2023-04-13
schemaClass	Summation
text	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.

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