Format

Send to

Choose Destination
See comment in PubMed Commons below
Virology. 2013 Jan 20;435(2):493-503. doi: 10.1016/j.virol.2012.10.024. Epub 2012 Nov 6.

Endoplasmic reticulum export and vesicle formation of the movement protein of Chinese wheat mosaic virus are regulated by two transmembrane domains and depend on the secretory pathway.

Author information

  • 1State Key Laboratory Breeding Base for Zhejiang Sustainable Pest and Disease Control, Ministry of Agriculture Key Laboratory of Biotechnology in Plant Protection, Institute of Virology and Biotechnology, Zhejiang Academy of Agricultural Sciences, Hangzhou 310021, PR China.

Abstract

The 37K protein of Chinese wheat mosaic virus (CWMV) belongs to the 30K superfamily of plant virus movement proteins. CWMV 37K trans-complemented the cell-to-cell spread of a movement-defective Potato virus X. CWMV 37K fused to enhanced green fluorescent protein localized to plasmodesmata and formed endoplasmic reticulum (ER)-derived vesicular and large aggregate structures. CWMV 37K has two putative N-terminal transmembrane domains (TMDs). Mutations disrupting TMD1 or TMD2 impaired 37K movement function; those mutants were unable to form ER-derived structures but instead accumulated in the ER. Treatment with Brefeldin A or overexpression of the dominant negative mutant of Sar1 retained 37K in the ER, indicating that ER export of 37K is dependent on the secretory pathway. Moreover, CWMV 37K interacted with pectin methylesterases and mutations in TMD1 or TMD2 impaired this interaction in planta. The results suggest that the two TMDs regulate the movement function and intracellular transport of 37K.

PMID:
23137810
DOI:
10.1016/j.virol.2012.10.024
[PubMed - indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center