ArticleFrontiers in plant science2011
PD Trafficking of Potato Leaf Roll Virus Movement Protein in Arabidopsis Depends on Site-specific Protein Phosphorylation.
Article in Frontiers in plant science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 34 citations in OpenAlex.
- Barley GRIK1-SnRK1 kinases subvert a viral virulence protein to upregulate antiviral RNAi and inhibit infection.The EMBO journal · 2022Article
- Phosphorylation of plant virus proteins: Analysis methods and biological functions.Frontiers in microbiology · 2022Review
- Article
- Phosphorylations of the Abutilon Mosaic Virus Movement Protein Affect Its Self-Interaction, Symptom Development, Viral DNA Accumulation, and Host Range.Frontiers in plant science · 2020Article
- Brassica yellows virus' movement protein upregulates anthocyanin accumulation, leading to the development of purple leaf symptoms on Arabidopsis thaliana.Scientific reports · 2018Article
- Article
- Phosphorylation coexists with O-GlcNAcylation in a plant virus protein and influences viral infection.Molecular plant pathology · 2018Article
- The enemy within: phloem-limited pathogens.Molecular plant pathology · 2018Review
- Phosphorylation regulates the subcellular localization of Cucumber Mosaic Virus 2b protein.Scientific reports · 2017Article
- Localization ofThe plant pathology journal · 2017Article
- Phosphorylation of TGB1 by protein kinase CK2 promotes barley stripe mosaic virus movement in monocots and dicots.Journal of experimental botany · 2015Article
- Evidence for lysine acetylation in the coat protein of a polerovirus.The Journal of general virology · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many plant viruses encode for specialized movement proteins (MP) to facilitate passage of viral material to and through plasmodesmata (PD). To analyze intracellular trafficking of potato leaf roll virus (PLRV) movement protein (MP17) we performed GFP fusion experiments with distinct deletion variants of MP17. These studies revealed that the C-terminus of MP17 is essential but not sufficient for PD targeting. Interestingly, fusion of GFP to three C-terminal MP17 deletion variants resulted in the accumulation of GFP in chloroplasts. This indicates that MP17 harbors hidden plastid targeting sequences. Previous studies showed that posttranslational protein phosphorylation influences PD targeting of MP and virus spread. Analysis of MP17-derived phospho-peptides by mass spectrometry revealed four phosphorylated serine residues (S71, S79, S137, and S140). Site-directed mutagenesis of S71/S79 and S137/S140 showed that the C-terminal serine residues S137/S140 are dispensable for PD targeting. However, exchange of S71/S79 to A71/A79 abolished PD targeting of the mutated MP17 protein. To mimic phosphorylation of S71/S79 both amino acids were substituted by aspartic acid. The resulting D71/D79 variant of MP17 was efficiently targeted to PD. Further deletion analysis showed that PD targeting of MP17 is dependent on the C-terminus, phosphorylation of S71 and/or S79 and a N-terminal domain.
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