title: Plasma membrane protein ubiquitylation and degradation as determinants of positional growth in plants.
abstract: Being sessile organisms, plants evolved an unparalleled plasticity in their post-embryonic development, allowing them to adapt and fine-tune their vital parameters to an ever-changing environment. Crosstalk between plants and their environment requires tight regulation of information exchange at the plasma membrane (PM). Plasma membrane proteins mediate such communication, by sensing variations in nutrient availability, external cues as well as by controlled solute transport across the membrane border. Localization and steady-state levels are essential for PM protein function and ongoing research identified cis- and trans-acting determinants, involved in control of plant PM protein localization and turnover. In this overview, we summarize recent progress in our understanding of plant PM protein sorting and degradation via ubiquitylation, a post-translational and reversible modification of proteins. We highlight characterized components of the machinery involved in sorting of ubiquitylated PM proteins and discuss consequences of protein ubiquitylation on fate of selected PM proteins. Specifically, we focus on the role of ubiquitylation and PM protein degradation in the regulation of polar auxin transport (PAT). We combine this regulatory circuit with further aspects of PM protein sorting control, to address the interplay of events that might control PAT and polarized growth in higher plants.
authors: Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna (BOKU), Muthgasse 18, 1190, Vienna, Austria.
authors: Barbara
authors: B
authors: Korbei
authors: Christian
authors: C
authors: Luschnig
mesh_terms: D002462:Cell Membrane / Q000378:metabolism*; D004705:Endocytosis; D008565:Membrane Proteins / Q000378:metabolism*; D063245:Plant Development; D059748:Proteolysis; D054875:Ubiquitination
chemical_list: D008565:Membrane Proteins
keywords: Arabidopsis; PIN protein; auxin; protein degradation; ubiquitin