The matrix protein of vesicular stomatitis virus inhibits nucleocytoplasmic transport when it is in the nucleus and associated with nuclear pore complexes

J. M. Petersen, L. S. Her, V. Varvel, E. Lund, J. E. Dahlberg

Research output: Contribution to journalArticlepeer-review

131 Citations (Scopus)

Abstract

The matrix (M) protein of vesicular stomatitis virus (VSV) is a potent inhibitor of bidirectional nuclear transport. Here we demonstrate that inhibition occurs when M protein is in the nucleus of Xenopus laevis oocytes and that M activity is readily reversed by a monoclonal antibody (αM). We identify a region of M protein, amino acids 51 to 59, that is required both for inhibition of transport and for efficient recognition by αM. When expressed in transfected HeLa cells, M protein colocalizes with nuclear pore complexes (NPCs) at the nuclear rim. Moreover, mutation of a single amino acid, methionine 51, eliminates both transport inhibition and targeting to NPCs. We propose that M protein inhibits bidirectional transport by interacting with a component of the NPC or an NPC-associated factor that participates in nucleocytoplasmic transport.

Original languageEnglish
Pages (from-to)8590-8601
Number of pages12
JournalMolecular and Cellular Biology
Volume20
Issue number22
DOIs
Publication statusPublished - 2000 Nov 11

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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