Vacuolar Degradation of Two Integral Plasma Membrane Proteins, AtLRR84A and OsSCAMP1, Is Cargo Ubiquitination-Independent and Prevacuolar Compartment-Mediated in Plant Cells
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AbstractIn plant cells, how integral plasma membrane (PM) proteins are degraded in a cargo ubiquitination-independent manner remains elusive. Here, we studied the degradative pathway of two plant PM proteins: AtLRR84A, a type I integral membrane protein belonging to the leucine-rich repeat receptor-like kinase protein family, and OsSCAMP1 (rice secretory carrier membrane protein 1), a tetraspan transmembrane protein located on the PM and trans-Golgi network (TGN) or early endosome (EE). Using wortmannin and ARA7(Q69L) mutant that could enlarge the multivesicular body (MVB) or prevacuolar compartment (PVC) as tools, we demonstrated that, when expressed as green fluorescent protein (GFP) fusions in tobacco BY-2 or Arabidopsis protoplasts, both AtLRR84A and OsSCAMP1 were degraded in the lytic vacuole via the internal vesicles of MVB/PVC in a cargo ubiquitination-independent manner. Such MVB/PVC-mediated vacuolar degradation of PM proteins was further supported by immunocytochemical electron microscopy (immunoEM) study showing the labeling of the fusions on the internal vesicles of the PVC/MVB. Thus, cargo ubiquitination-independent and PVC-mediated degradation of PM proteins in the vacuole is functionally operated in plant cells.
All Author(s) ListCai Y, Zhuang XH, Wang JQ, Wang H, Lam SK, Gao CJ, Wang XF, Jiang LW
Journal nameTRAFFIC
Year2012
Month7
Day1
Volume Number13
Issue Number7
PublisherWiley: 12 months
Pages1023 - 1040
ISSN1398-9219
eISSN1600-0854
LanguagesEnglish-United Kingdom
Keywordsmultivesicular body; plasma membrane protein; prevacuolar compartment; ubiquitination; vacuolar degradation
Web of Science Subject CategoriesCell Biology; CELL BIOLOGY

Last updated on 2020-26-01 at 23:34