High impact information on VPS30

• Here we show that plant BECLIN 1, an ortholog of the yeast and mammalian autophagy gene ATG6/VPS30/beclin 1, functions to restrict HR PCD to infection sites [1].
• These results indicate that Vps30p functions as a subunit of a Vps34 PtdIns 3-kinase complex(es) [2].
• Although Vps30p is known to interact with Apg14p, its precise role remains unclear [2].
• The sequences of the VPS29, VPS30, and VPS35 genes do not yet give any clues to the functions of their products [3].
• Vps34p and Vps30p, components shared by the two complexes, localized to the PAS, vacuolar membranes, and several punctate structures that included endosomes [4].

Biological context of VPS30

• We observed that mutations in the VPS30 and VPS38 genes led to a selective sorting and maturation phenotype of the soluble vacuolar protease CPY [5].
• Apg14p and Apg6/Vps30p form a protein complex essential for autophagy in the yeast, Saccharomyces cerevisiae [6].
• These results imply that Apg6/Vps30p has two distinct functions in the autophagic process and the vacuolar protein sorting pathway [6].
• Using nematodes with a loss-of-function mutation in the insulin-like signaling pathway, we show that bec-1, the C. elegans ortholog of the yeast and mammalian autophagy gene APG6/VPS30/beclin1, is essential for normal dauer morphogenesis and life-span extension [7].

Associations of VPS30 with chemical compounds

• The defect in one of these mutants, add3, was complemented by VPS30/ATG6, a gene that encodes a component of two phosphatidylinositol 3-kinase (PtdIns 3-kinase) complexes: complex I is required for autophagy, whereas complex II is required for the carboxypeptidase Y (CPY)-to-vacuole pathway [8].

Physical interactions of VPS30

• Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex [6].

Other interactions of VPS30

• Subcellular fractionation indicated that Apg14p and Apg6p peripherally associated with a membrane structure(s) [6].
• The distribution of a green fluorescent protein fusion of the autophagosome marker, Atg8, is aberrant in both atg1-1 and atg6(-) mutants [9].

References