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Feraru, E, Paciorek, T, Feraru, MI, Zwiewka, M, De Groodt, R, De Rycke, R, Kleine-Vehn, J and Friml, J (2010) The AP-3 β adaptin mediates the biogenesis and function of lytic vacuoles in Arabidopsis. Plant Cell 22:2812-24


Plant vacuoles are essential multifunctional organelles largely distinct from similar organelles in other eukaryotes. Embryo protein storage vacuoles and the lytic vacuoles that perform a general degradation function are the best characterized, but little is known about the biogenesis and transition between these vacuolar types. Here, we designed a fluorescent marker-based forward genetic screen in Arabidopsis thaliana and identified a protein affected trafficking2 (pat2) mutant, whose lytic vacuoles display altered morphology and accumulation of proteins. Unlike other mutants affecting the vacuole, pat2 is specifically defective in the biogenesis, identity, and function of lytic vacuoles but shows normal sorting of proteins to storage vacuoles. PAT2 encodes a putative β-subunit of adaptor protein complex 3 (AP-3) that can partially complement the corresponding yeast mutant. Manipulations of the putative AP-3 β adaptin functions suggest a plant-specific role for the evolutionarily conserved AP-3 β in mediating lytic vacuole performance and transition of storage into the lytic vacuoles independently of the main prevacuolar compartment-based trafficking route.


PubMed PMC2947184 Online version:10.1105/tpc.110.075424


Adaptor Protein Complex 3/genetics; Adaptor Protein Complex 3/metabolism; Adaptor Protein Complex beta Subunits/genetics; Adaptor Protein Complex beta Subunits/metabolism; Arabidopsis/genetics; Arabidopsis/metabolism; Arabidopsis Proteins/genetics; Arabidopsis Proteins/metabolism; Cloning, Molecular; Mutation; Protein Transport; Vacuoles/metabolism



Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status



GO:0080171: lytic vacuole organization

ECO:0000315: mutant phenotype evidence used in manual assertion


Seeded From UniProt


See also


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