Journal
JOURNAL OF CELL SCIENCE
Volume 129, Issue 19, Pages 3597-3608Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.190082
Keywords
COPII; Erv14; Viral replication protein targeting; Protein perinuclear ER localization; Positive-strand RNA viruses; Viral replication complexes
Categories
Funding
- US-Israel Binational Science Foundation (BSF) [2013101]
- Virginia Tech Startup
- National Science Foundation (NSF) [1265260]
- Direct For Biological Sciences
- Division Of Integrative Organismal Systems [1265260] Funding Source: National Science Foundation
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Positive-strand RNAviruses invariably assemble their viral replication complexes (VRCs) by remodeling host intracellular membranes. How viral replication proteins are targeted to specific organelle membranes to initiate VRC assembly remains elusive. Brome mosaic virus (BMV), whose replication can be recapitulated in Saccharomyces cerevisiae, assembles its VRCs by invaginating the outer perinuclear endoplasmic reticulum (ER) membrane. Remarkably, BMV replication protein 1a (BMV 1a) is the only viral protein required for such membrane remodeling. We show that ER-vesicle protein of 14 kD (Erv14), a cargo receptor of coat protein complex II (COPII), interacts with BMV 1a. Moreover, the perinuclear ER localization of BMV 1a is disrupted in cells lacking ERV14 or expressing dysfunctional COPII coat components (Sec13, Sec24 or Sec31). The requirement of Erv14 for the localization of BMV 1a is bypassed by addition of a Sec24-recognizable sorting signal to BMV 1a or by overexpressing Sec24, suggesting a coordinated effort by both Erv14 and Sec24 for the proper localization of BMV 1a. The COPII pathway is well known for being involved in protein secretion; our data suggest that a subset of COPII coat proteins have an unrecognized role in targeting proteins to the perinuclear ER membrane.
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