Meiling-Wesse Khuyen, Barth Henning, Voss Christiane, Barmark Gunilla, Murén Eva, Ronne Hans, Thumm Michael
Institute of Biochemistry, University of Stuttgart, Pfaffenwaldring 55, Germany.
FEBS Lett. 2002 Oct 23;530(1-3):174-80. doi: 10.1016/s0014-5793(02)03456-7.
Here we identify Mon1p as being essential for the cvt-pathway and autophagy. Thus, mon1Delta cells are impaired in proaminopeptidase I maturation and homozygous diploid mon1Delta cells do not sporulate. Quantitative autophagy measurements suggest a complete autophagy block. The autophagosomal marker protein GFP-Aut7p accumulates in mon1Delta cells at punctate structures outside the vacuole. Furthermore, proaminopeptidase I accumulates in mon1Delta cells in a proteinase-protected form. Our data demonstrate that mon1Delta cells are defective in the fusion of cvt-vesicles and autophagosomes with the vacuole. Consistent with this, GFP-Mon1p localizes to the cytosol and to punctate structures within the cytosol.
在此，我们确定Mon1p对于液泡蛋白分选转运途径（cvt途径）和自噬至关重要。因此，mon1Δ细胞在氨肽酶I成熟过程中受损，纯合二倍体mon1Δ细胞不能形成孢子。定量自噬测量表明存在完全的自噬阻断。自噬体标记蛋白GFP-Aut7p在mon1Δ细胞的液泡外点状结构中积累。此外，氨肽酶I以蛋白酶保护的形式在mon1Δ细胞中积累。我们的数据表明，mon1Δ细胞在cvt小泡和自噬体与液泡的融合方面存在缺陷。与此一致的是，GFP-Mon1p定位于细胞质和细胞质内的点状结构。
