Journal
PLANT SIGNALING & BEHAVIOR
Volume 10, Issue 2, Pages -Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/15592324.2014.984524
Keywords
arabinogalactan proteins; exocyst-positive organelle; glycosyltransferases; protein O-glycosylation; plant proteoglycan; plant cell wall; unconventional protein secretion
Categories
Funding
- Danish Agency for Science, Technology and Innovation: the Strategic Research for Health, Food and Welfare [DSF:09-067059]
- Danish Agency for Science, Technology and Innovation: the Technology and Production [FTP:274-09-0113]
Ask authors/readers for more resources
Arabinogalactan proteins are abundant cell surface proteoglycans in plants and are implicated to act as developmental markers during plant growth. We previously reported that AtGALT31A, AtGALT29A, and AtGLCAT14A-C, which are involved in the biosynthesis of arabinogalactan proteins, localize not only to the Golgi cisternae but also to smaller compartments, which may be a part of the unconventional protein secretory pathway in plants. In Poulsen et al., 1 we have demonstrated increased targeting of AtGALT29A to small compartments when Y144 is substituted with another amino acid, and we implicated a role for Y144 in the subcellular targeting of AtGALT29A. In this paper, we are presenting another aspect of Y144 substitution in AtGALT29A; namely, Y144A construct demonstrated a 2.5-fold increase while Y144E construct demonstrated a 2-fold decrease in the galactosyltransferase activity of AtGALT29A. Therefore, the electrostatic status of Y144, which is regulated by an unknown kinase/phosphatase system, may regulate AtGALT29A enzyme activity. Moreover, we have identified additional proteins, apyrase 3 (APY3; At1g14240) and UDPglucuronate epimerases 1 and 6 (GAE1, At4g30440; GAE6, At3g23820), from Arabidopsis thaliana that co-localize with AtGALT31A in the small compartments when expressed transiently in Nicotiana benthamiana. These proteins may play roles in nucleotide sugar metabolism in the small compartments together with arabinogalactan glycosyltransferases.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available