The tonoplast--where sweetness is dispensable.

is involved in negative feedback regulation of the gibberellic acid biosynthetic pathway in rice (Oryza sativa). 2013. The rice narrow leaf2 and narrow leaf3 loci encode WUSCHEL-related homeobox 3A (OsWOX3A) and function in leaf, spikelet, tiller and lateral root development. conserved repressive activity of WOX proteins mediates leaf blade outgrowth and floral organ development in plants. The maize duplicate genes narrow sheath1 and narrow sheath2 encode a conserved homeobox gene function in a lateral domain of shoot apical meristems. a WUSCHEL-like Homeobox gene, is required for lateral fusion of floral organs in Medicago truncatula. STENOFOLIA recruits TOPLESS to repress ASYMMETRIC LEAVES2 at the leaf margin and promote leaf blade outgrowth in Medicago truncatula. Homeobox1 transcription factor, controls organ lateral growth, and regulates tendril and dorsal petal identities in garden pea (Pisum sativum L. The proteolytic machinery of certain cellular organelles is potentially harmful to resident proteins. In mammals , the large luminal domains of integral lysosomal proteins are heavily glycosylated to protect them from degradation. In this issue of Journal of Experimental Botany (pages 1769–1781) Pedrazzini and co-workers reveal that plants are very different. Glycosylation is one of the most common protein modifications in all eukaryotes. Resident proteins of different intracel-lular organelles including the endoplasmic reticulum (ER), Golgi apparatus and hydrolysing compartments are often glycosylated at multiple sites with oligosaccharide chains of varying length and composition. The attached carbohydrates modulate protein stability, activity and trafficking and mediate protein–protein interactions. N-glycosylation, the most prevalent form of protein glycosylation in eukaryotes, is defined by the covalent linkage of an oligosaccharide (N-glycan) to selected asparagine residues of newly synthesized secretory proteins as they are translocated into the ER. Once attached to the polypeptide chain, the N-glycans play crucial roles in protein folding and quality control processes (Helenius and Aebi, 2001) – for example, they regulate a specific cell death event in Arabidopsis (de Oliveira et al., 2016). Immediately after the transfer to the protein, N-glycans are subjected to step-wise processing reactions that alter the composition of the N-glycan and by doing so control the fate of glycoproteins. As a consequence, the exposure of a defined permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.