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Vol. 11, Issue 1, 13-22, January 2000
Department of Cell Biology and Anatomy, The Johns Hopkins
University School of Medicine, Baltimore, Maryland 21205
The vesicular stomatitis virus (VSV) G protein is a model
transmembrane glycoprotein that has been extensively used to study the
exocytotic pathway. A signal in the cytoplasmic tail of VSV G (DxE or
Asp-x-Glu, where x is any amino acid) was recently proposed to mediate
efficient export of the protein from the endoplasmic reticulum (ER). In
this study, we show that the DxE motif only partially accounts for
efficient ER exit of VSV G. We have identified a six-amino-acid signal,
which includes the previously identified Asp and Glu residues, that is
required for efficient exit of VSV G from the ER. This six-residue
signal also includes the targeting sequence YxxØ (where x is any amino
acid and Ø is a bulky, hydrophobic residue) implicated in several
different sorting pathways. The only defect in VSV G proteins with
mutations in the six-residue signal is slow exit from the ER; folding
and oligomerization in the ER are normal, and the mutants eventually
reach the plasma membrane. Addition of this six-residue motif to an
inefficiently transported reporter protein is sufficient to confer an
enhanced ER export rate. The signal we have identified is highly
conserved among divergent VSV G proteins, and we suggest this reflects
the importance of this motif in the evolution of VSV G as a proficient exocytic protein.
Corresponding author. E-mail address:
machamer{at}bs.jhmi.edu.
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