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Choline transporter-like1 is required for plasmodesmal targeting of Potato leafroll virus movement protein MP17 and long-distance assimilate transport

ABSTRACT: Macromolecular trafficking and cell-to-cell communication in plants occurs via plasmodesmata (PD). Currently, little is known about the proteins defining these sophisticated cell-to-cell contacts. To uncover proteins required for PD structure and function we made use of the 17 kDa movement protein (MP17) of the Potato leafroll virus (PLRV). The protein is required for cell-to-cell movement of the virus and localizes specifically to branched PD in source tissues. By forward genetic screening for Arabidopsis mutants with altered PD binding of MP17, several mutants were found. Map-based cloning of one of these mutants revealed a mutation in the choline transporter-like 1 (CHER1) protein. The mutation abolished plasma membrane localization of the protein. As consequence phosphatidylcholine levels and PD binding of MP17 decreased. Transcriptome analysis revealed a down-regulation of defense genes and genes involved in the synthesis of very long chain fatty acids, indicating an impairment of lipid signaling. Furthermore, cher1 mutants showed a reduced assimilate export and stunted growth. These findings highlight the emerging role of phospholipids, especially in the context of PD structure and function as well as potential binding sites for plasma membrane- and PD-associated proteins, which has been neglected for a long time.

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE61595 | GEO | 2016/06/01

SECONDARY ACCESSION(S): PRJNA261631

REPOSITORIES: GEO

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Choline transporter-like1 is required for plasmodesmal targeting of Potato leafroll virus movement protein MP17 and long-distance assimilate transport

Project description:Macromolecular trafficking and cell-to-cell communication in plants occurs via plasmodesmata (PD). Currently, little is known about the proteins defining these sophisticated cell-to-cell contacts. To uncover proteins required for PD structure and function we made use of the 17 kDa movement protein (MP17) of the Potato leafroll virus (PLRV). The protein is required for cell-to-cell movement of the virus and localizes specifically to branched PD in source tissues. By forward genetic screening for Arabidopsis mutants with altered PD binding of MP17, several mutants were found. Map-based cloning of one of these mutants revealed a mutation in the choline transporter-like 1 (CHER1) protein. The mutation abolished plasma membrane localization of the protein. As consequence phosphatidylcholine levels and PD binding of MP17 decreased. Transcriptome analysis revealed a down-regulation of defense genes and genes involved in the synthesis of very long chain fatty acids, indicating an impairment of lipid signaling. Furthermore, cher1 mutants showed a reduced assimilate export and stunted growth. These findings highlight the emerging role of phospholipids, especially in the context of PD structure and function as well as potential binding sites for plasma membrane- and PD-associated proteins, which has been neglected for a long time. light exposed source leaves from wild type Col-0, T-DNA insertion line cher1-4 and mutant cher1-5 (10 weeks old). Samples: per pool 2 source leaves from 4 different plants, taken in the afternoon; wildtype (WT): Col-0, cher1-4: T-DNA insertion line SALK-065853 (ecotype Col-0, kanamycin resistance), cher1-5: Col-0 with GGA -->GAA at position 740 of cds

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Expression profiles of embryo-defective Arabidopsis thaliana mutants increased size exclusion limit1 (ise1) and ise2

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2019-07-08 | PXD013999 | Pride

A balance in the delivery of ER components and the vacuolar proton pump determines phagosome acidification

Project description:As part of a study comparing phagosome composition in wild-type Dictyostelium discoideum with mutants in two cytoskeletal/motor proteins, we compared global gene expression and proteomes between the strains to test whether differences in mRNA and protein abundance were correlated with changes in phagosomal composition. abp1 and myoK mutants in both the Ax2 and DH1 backgrounds were compared with their respective wild-type parents.Both analyses converged and confirmed the phagosome analysis (supplemental Tables). Protein differences were markedly fewer in the myoK-null mutant than in the abp1 null lysate. Proteins of known function, differential in the myoK-null lysate, were involved in remodeling of the plasma membrane and early membrane trafficking. Proteins differential in the abp1-null lysate spanned various functions at all levels of cell metabolism. Most of the proteins differential in 2D-DIGE displayed similar mutant-to-wt ratios at the mRNA level in microarrays. A prominent example of overlap is the 1.4 fold overexpression (p ??? 0.016) of Vps5, both in proteomics and microarray analyses of abp1-null cells. Like half of the proteins involved in membrane trafficking that are differential in microarray analyses of abp1-null cells, Vps5 is putatively involved in endosome-to-Golgi trafficking as a retromer sorting nexin. Therefore, one might speculate that, in addition to direct effects on phagocytic uptake, absence of Abp1 has an impact on endosome-to-Golgi trafficking.

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