Reactome | Nascent F signal peptide is cleaved at ER membrane

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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Disease (Homo sapiens)

- Infectious disease (Homo sapiens)
  - Viral Infection Pathways (Homo sapiens)
    - Respiratory Syncytial Virus Infection Pathway (Homo sapiens)
      - Respiratory syncytial virus (RSV) genome replication, transcription and translation (Homo sapiens)
        
        Maturation of hRSV A proteins (Homo sapiens)
        
        Nascent F signal peptide is cleaved at ER membrane (Homo sapiens)

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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 McGraw, PA, Crowe, JE, Heck, JM, Brock, SC	J Virol	2005
4031826	Kinetics of synthesis of respiratory syncytial virus glycoproteins Gerin, JL, Fernie, BF, Cote, PJ, Dapolito, G	J Gen Virol	1985