Cvt9/Gsa9 Functions in Sequestering Selective Cytosolic Cargo Destined for the Vacuole

التفاصيل البيبلوغرافية
العنوان: Cvt9/Gsa9 Functions in Sequestering Selective Cytosolic Cargo Destined for the Vacuole
المؤلفون: Ann Hefner-Gravink, Yoshinori Ohsumi, Ju Guan, Yoshiaki Kamada, Daniel J. Klionsky, Misuzu Baba, John Kim, Per E. Stromhaug, Sidney V. Scott, William A. Dunn
المصدر: The Journal of Cell Biology
بيانات النشر: Rockefeller University Press, 2001.
سنة النشر: 2001
مصطلحات موضوعية: autophagy, Saccharomyces cerevisiae Proteins, Recombinant Fusion Proteins, Blotting, Western, Macropexophagy, Saccharomyces cerevisiae, Vacuole, CVT pathway, Biology, Cell Fractionation, Aminopeptidases, Pichia, Cytosol, Lysosome, Peroxisomes, medicine, Humans, peroxisome, Protein Precursors, Transport Vesicles, degradation, Cytoplasm-to-vacuole targeting, vacuole, Cell Membrane, Autophagy, Biological Transport, Cell Biology, Cell biology, Glucose, medicine.anatomical_structure, Microscopy, Fluorescence, Vacuoles, lysosome, Micropexophagy, Original Article, Carrier Proteins, Plasmids, Protein Binding, Signal Transduction
الوصف: Three overlapping pathways mediate the transport of cytoplasmic material to the vacuole in Saccharomyces cerevisiae. The cytoplasm to vacuole targeting (Cvt) pathway transports the vacuolar hydrolase, aminopeptidase I (API), whereas pexophagy mediates the delivery of excess peroxisomes for degradation. Both the Cvt and pexophagy pathways are selective processes that specifically recognize their cargo. In contrast, macroautophagy nonselectively transports bulk cytosol to the vacuole for recycling. Most of the import machinery characterized thus far is required for all three modes of transport. However, unique features of each pathway dictate the requirement for additional components that differentiate these pathways from one another, including at the step of specific cargo selection.We have identified Cvt9 and its Pichia pastoris counterpart Gsa9. In S. cerevisiae, Cvt9 is required for the selective delivery of precursor API (prAPI) to the vacuole by the Cvt pathway and the targeted degradation of peroxisomes by pexophagy. In P. pastoris, Gsa9 is required for glucose-induced pexophagy. Significantly, neither Cvt9 nor Gsa9 is required for starvation-induced nonselective transport of bulk cytoplasmic cargo by macroautophagy. The deletion of CVT9 destabilizes the binding of prAPI to the membrane and analysis of a cvt9 temperature-sensitive mutant supports a direct role of Cvt9 in transport vesicle formation. Cvt9 oligomers peripherally associate with a novel, perivacuolar membrane compartment and interact with Apg1, a Ser/Thr kinase essential for both the Cvt pathway and autophagy. In P. pastoris Gsa9 is recruited to concentrated regions on the vacuole membrane that contact peroxisomes in the process of being engulfed by pexophagy. These biochemical and morphological results demonstrate that Cvt9 and the P. pastoris homologue Gsa9 may function at the step of selective cargo sequestration.
تدمد: 1540-8140
0021-9525
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7720f316ba8b563fe13b64b94ab9ea5Test
https://doi.org/10.1083/jcb.153.2.381Test
حقوق: OPEN
رقم الانضمام: edsair.doi.dedup.....c7720f316ba8b563fe13b64b94ab9ea5
قاعدة البيانات: OpenAIRE