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Cvt Pathway (cvt + pathway)
Selected AbstractsAtg17 recruits Atg9 to organize the pre-autophagosomal structureGENES TO CELLS, Issue 5 2009Takayuki Sekito Autophagy is a degradation system of cytoplasmic proteins and organelles via formation of double-membrane vesicles called autophagosomes. In the yeast Saccharomyces cerevisiae, autophagosomes are formed via the pre-autophagosomal structure (PAS) in a manner dependent on Atg proteins. Under nutrient-rich condition, Atg9 is recruited to the PAS by binding to Atg11 for the Cvt pathway. However, because Atg9 is recruited to the PAS in atg11, cells in starved condition and autophagy is induced, autophagy-specific mechanism for the Atg9 recruitment to the PAS has been assumed. Here, we demonstrate that, in autophagy-inducing condition, Atg9 is recruited to the PAS in a manner dependent on Atg17. Atg9 physically interacts with Atg17 in the presence of rapamycin. This interaction requires Atg1, a protein kinase essential for autophagy. Consistently, the Atg17-dependent PAS localization of Atg9 requires Atg1. However, its kinase activity is dispensable for this process. It rather regulates the equilibrium of assembly and disassembly of Atg9 at the PAS. [source] Crystallization of Saccharomyces cerevisiae,-mannosidase, a cargo protein of the Cvt pathwayACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 6 2009Yasunori Watanabe Saccharomyces cerevisiae,-mannosidase (Ams1) is a cargo protein that is transported to the vacuole by the cytoplasm-to-vacuole targeting (Cvt) pathway during conditions of growth and by autophagy during conditions of starvation. After transport to the vacuole, Ams1 functions as a resident hydrolase. Ams1 has been overexpressed in the methylotrophic yeast Pichia pastoris, purified and crystallized in two crystal forms. Form I belongs to space group P21, with unit-cell parameters a = 145.7, b = 127.7, c = 164.0,Å, , = 101.5°. Form II belongs to space group I222 or I212121, with unit-cell parameters a = 127.9, b = 163.7, c = 291.5,Å. Diffraction data were collected from these crystals to a resolution of 3.3,Å for form I and of 2.6,Å for form II using synchrotron radiation. [source] Crystallization of Saccharomyces cerevisiae aminopeptidase 1, the major cargo protein of the Cvt pathwayACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 3 2007Wakana Adachi The vacuole hydrolase aminopeptidase 1 (Ape1) is a cargo protein transported to the vacuole by the cytosol-to-vacuole targeting (Cvt) pathway during conditions of growth and by autophagy during conditions of starvation. After transport to the vacuole, Ape1 is processed into mature Ape1 (mApe1). mApe1 has been expressed, purified and crystallized in two crystal forms. Form I belongs to space group P21, with unit-cell parameters a = 120.6, b = 219.5, c = 133.1,Å, , = 116.5°. Form II belongs to space group R3, with unit-cell parameters a = 141.2, c = 349.4,Å. Diffraction data were collected from these crystals to a resolution of 2.5,Å for form I and 1.83,Å for form II. Self-rotation functions and the volume-to-weight ratio values suggest that forms I and II contain 12 and four mApe1 molecules per asymmetric unit, respectively, and that mApe1 exists as a tetrahedral dodecamer in both crystal forms. [source] Evidence for Yeast Autophagy during Simulation of Sparkling Wine Aging: A Reappraisal of the Mechanism of Yeast Autolysis in WineBIOTECHNOLOGY PROGRESS, Issue 2 2005Eduardo Cebollero Yeast autolysis is the source of several molecules responsible for the quality of wines aged in contact with yeast cells. However, the mechanisms of yeast autolysis during wine aging are not completely understood. All descriptions of yeast autolysis in enological conditions emphasize the disturbance of cell organization as the starting event in the internal digestion of the cell, while no reference to autophagy is found in wine-related literature. By using yeast mutants defective in the autophagic or the Cvt pathways we have demonstrated that autophagy does take place in wine production conditions. This finding has implications for the genetic improvement of yeasts for accelerated autolysis. [source] | ||||||||||