James Crowe
Faculty Member
Last active: 3/31/2020

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 79 (19): 12528-35

PMID: 16160180 · PMCID: PMC1211512 · DOI:10.1128/JVI.79.19.12528-12535.2005

The processes that facilitate transport of integral membrane proteins though the secretory pathway and subsequently target them to particular cellular membranes are relevant to almost every field of biology. These transport processes involve integration of proteins into the membrane of the endoplasmic reticulum (ER), passage from the ER to the Golgi, and post-Golgi trafficking. The respiratory syncytial virus (RSV) fusion (F) protein is a type I integral membrane protein that is uniformly distributed on the surface of infected nonpolarized cells and localizes to the apical plasma membrane of polarized epithelial cells. We expressed wild-type or altered RSV F proteins to gain a better understanding of secretory transport and plasma membrane targeting of type I membrane proteins in polarized and nonpolarized epithelial cells. Our findings reveal a novel, orientation-independent apical plasma membrane targeting function for the transmembrane domain of the RSV F protein in polarized epithelial cells. This work provides a basis for a more complete understanding of the role of the transmembrane domain and cytoplasmic tail of viral type I integral membrane proteins in secretory transport and plasma membrane targeting in polarized and nonpolarized cells.

MeSH Terms (18)

Animals Cell Line Cell Line, Tumor Cell Membrane Cell Polarity Dogs Epithelial Cells Genes, Reporter Green Fluorescent Proteins Humans Microscopy, Confocal Mutation Protein Sorting Signals Protein Structure, Tertiary Recombinant Fusion Proteins Respiratory Syncytial Viruses Sequence Deletion Viral Fusion Proteins

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