Golgi maturation visualized in living yeast. 2006

Eugene Losev, and Catherine A Reinke, and Jennifer Jellen, and Daniel E Strongin, and Brooke J Bevis, and Benjamin S Glick
Department of Molecular Genetics and Cell Biology, and Institute for Biophysical Dynamics, The University of Chicago, 920 East 58th Street, Chicago, Illinois 60637, USA.

The Golgi apparatus is composed of biochemically distinct early (cis, medial) and late (trans, TGN) cisternae. There is debate about the nature of these cisternae. The stable compartments model predicts that each cisterna is a long-lived structure that retains a characteristic set of Golgi-resident proteins. In this view, secretory cargo proteins are transported by vesicles from one cisterna to the next. The cisternal maturation model predicts that each cisterna is a transient structure that matures from early to late by acquiring and then losing specific Golgi-resident proteins. In this view, secretory cargo proteins traverse the Golgi by remaining within the maturing cisternae. Various observations have been interpreted as supporting one or the other mechanism. Here we provide a direct test of the two models using three-dimensional time-lapse fluorescence microscopy of the yeast Saccharomyces cerevisiae. This approach reveals that individual cisternae mature, and do so at a consistent rate. In parallel, we used pulse-chase analysis to measure the transport of two secretory cargo proteins. The rate of cisternal maturation matches the rate of protein transport through the secretory pathway, suggesting that cisternal maturation can account for the kinetics of secretory traffic.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008856 Microscopy, Fluorescence Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye. Fluorescence Microscopy,Immunofluorescence Microscopy,Microscopy, Immunofluorescence,Fluorescence Microscopies,Immunofluorescence Microscopies,Microscopies, Fluorescence,Microscopies, Immunofluorescence
D008954 Models, Biological Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment. Biological Model,Biological Models,Model, Biological,Models, Biologic,Biologic Model,Biologic Models,Model, Biologic
D002268 Carboxypeptidases Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue. Carboxypeptidase
D006056 Golgi Apparatus A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990) Golgi Complex,Apparatus, Golgi,Complex, Golgi
D012441 Saccharomyces cerevisiae A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement. Baker's Yeast,Brewer's Yeast,Candida robusta,S. cerevisiae,Saccharomyces capensis,Saccharomyces italicus,Saccharomyces oviformis,Saccharomyces uvarum var. melibiosus,Yeast, Baker's,Yeast, Brewer's,Baker Yeast,S cerevisiae,Baker's Yeasts,Yeast, Baker
D043402 Cathepsin A A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13. Carboxypeptidase C,Carboxypeptidase Y,Lysosomal Protective Protein,Acid Carboxypeptidase,BGPP,Endothelin Degradation Enzyme,Serine Carboxypeptidase I,beta-Galactosidase Protective Protein,beta Galactosidase Protective Protein
D018613 Microscopy, Confocal A light microscopic technique in which only a small spot is illuminated and observed at a time. An image is constructed through point-by-point scanning of the field in this manner. Light sources may be conventional or laser, and fluorescence or transmitted observations are possible. Confocal Microscopy,Confocal Microscopy, Scanning Laser,Laser Microscopy,Laser Scanning Confocal Microscopy,Laser Scanning Microscopy,Microscopy, Confocal, Laser Scanning,Confocal Laser Scanning Microscopy,Confocal Microscopies,Laser Microscopies,Laser Scanning Microscopies,Microscopies, Confocal,Microscopies, Laser,Microscopies, Laser Scanning,Microscopy, Laser,Microscopy, Laser Scanning,Scanning Microscopies, Laser,Scanning Microscopy, Laser
D018715 Microscopy, Video Microscopy in which television cameras are used to brighten magnified images that are otherwise too dark to be seen with the naked eye. It is used frequently in TELEPATHOLOGY. Video Microscopy,Videomicrography,Videomicroscopy,Microscopies, Video,Video Microscopies,Videomicrographies,Videomicroscopies
D020662 Guanine Nucleotide Exchange Factors Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS. GDP Exchange Factors,GDP-GTP Reversing Factors,Guanine Nucleotide Releasing Factors,GDP Dissociation Factor,GDP Dissociation Stimulators,GDP-GTP Exchange Protein,Guanine Nucleotide Exchange Factor,Guanine-Nucleotide-Releasing Factor,Exchange Factors, GDP,Factors, GDP Exchange,Factors, GDP-GTP Reversing,GDP GTP Exchange Protein,GDP GTP Reversing Factors,Guanine Nucleotide Releasing Factor,Reversing Factors, GDP-GTP

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