Format

Send to

Choose Destination
Int J Mol Sci. 2017 Apr 13;18(4). pii: E825. doi: 10.3390/ijms18040825.

Subcellular Localization of Arabidopsis Pathogenesis-Related 1 (PR1) Protein.

Author information

1
Laboratory of Cell Biology, Institute of Experimental Botany, Academy of Sciences of the Czech Republic, Rozvojova 263, 165 02 Prague 6, Czech Republic. pecenkova@ueb.cas.cz.
2
Laboratory of Cell Biology, Institute of Experimental Botany, Academy of Sciences of the Czech Republic, Rozvojova 263, 165 02 Prague 6, Czech Republic. pleskot@ueb.cas.cz.
3
Laboratory of Cell Morphogenesis, Department of Experimental Plant Biology, Faculty of Science, Charles University in Prague, Vinicna 5, 128 44 Prague 2, Czech Republic. zarsky@ueb.cas.cz.

Abstract

The Arabidopsisthaliana pathogenesis-related 1 (PR1) is an important defense protein, so far it has only been detected in extracellular space and its subcellular sorting and transport remain unexplained. Using a green fluorescent protein (GFP) tagged full length, as well as a C-terminus truncated version of PR1, we observed that when expressed ectopically in Nicotiana benthamiana leaves, PR1 co-localizes only partially with Golgi markers, and much more prominently with the late endosome (LE)/multivesicular body (MVB) FYVE marker. The C-truncated version PR1ΔC predominantly localized to the endoplasmic reticulum (ER). The same localizations were found for stable Arabidopsis transformants with expression of PR1 and PR1ΔC driven by the native promoter. We conclude that the A. thaliana PR1 (AtPR1) undergoes an unconventional secretion pathway, starting from the C-terminus-dependent sorting from the ER, and utilizing further transportation via phosphatidyl-inositol-3-phosphate (PI(3)P) positive LE/MVB-like vesicles. The homology model of the PR1 structure shows that the cluster of positively charged amino acid residues (arginines 60, 67, 137, and lysine 135) could indeed interact with negatively charged phospholipids of cellular membranes. It remains to be resolved whether Golgi and LE/MVB localization reflects an alternative sorting or trafficking succession, and what the role of lipid interactions in it will be.

KEYWORDS:

CAPE; MVB; PI(3)P; PR1; secretion; trafficking

PMID:
28406455
PMCID:
PMC5412409
DOI:
10.3390/ijms18040825
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Multidisciplinary Digital Publishing Institute (MDPI) Icon for PubMed Central
Loading ...
Support Center