Trafficking of ODV-E66 is mediated via a sorting motif and other viral proteins: Facilitated trafficking to the inner nuclear membrane

Sharon C. Braunagel, Shawn T. Williamson, Suraj Saksena, Zhenping Zhong, William Russell, David H. Russell, Max D. Summers

Research output: Contribution to journalArticle

75 Scopus citations

Abstract

The N-terminal 33 aa of the envelope protein ODV-E66 are sufficient to traffic fusion proteins to intranuclear membranes and the ODV envelope during infection with Autographa californica nucleopolyhedrovirus. This sequence has two distinct features: (i) an extremely hydrophobic sequence of 18 aa and (ii) positively charged amino acids close to the C-terminal end of the hydrophobic sequence. In the absence of infection, this sequence is sufficient to promote protein accumulation at the inner nuclear membrane. Covalent cross-linking results show that the lysines of the motif are proximal to FP25K and/or BV/ODV-E26 during transit from the endoplasmic reticulum to the nuclear envelope. We propose that the 33 aa comprise a signature for sorting proteins to the inner nuclear membrane (sorting motif) and that, unlike other resident proteins of the inner nuclear membrane, ODV-E66 and sorting-motif fusions do not randomly diffuse from their site of insertion at the endoplasmic reticulum to the nuclear envelope and viral-induced intranuclear membranes. Rather, during infection, trafficking is mediated by protein-protein interactions.

Original languageEnglish (US)
Pages (from-to)8372-8377
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume101
Issue number22
DOIs
StatePublished - Jun 1 2004
Externally publishedYes

    Fingerprint

ASJC Scopus subject areas

  • Genetics
  • General

Cite this