title: Cytochemical images of secretion in Saccharomyces cerevisiae and animal cells are different.
abstract: Like in animal cells, the major secretory pathway of the ascomycetous budding yeast Saccharomyces (s.) cerevisiae consists of membrane-bound compartments which transport soluble and membrane (glyco)peptides to lysosomal vacuoles, cell wall, or out of the cell. The established model of the cellular machinery of the yeast secretory pathway was deduced largerly from molecular ex situ analyses and for budding yeast cells it was assumed to be identical with that of secretory animal cells. Interphase yeast cells were never considered. Glycosylation of peptides was detected in the endoplasmic reticulum (ER) and the putative Golgi cisternae. Coated membrane vesicles were assumed to transport intermediates into and within the Golgi cascade. Proteolytic trimming would occur in the last Golgi compartment. Golgi-derived membrane vesicles would serve for exocytosis or fuse with lysosomal vacuoles. In contrast to this notion, yeast cytologists showed specific features of secretion in S. cerevisiae and other Ascomycetes. Cytochemical observations in situ of both dividing and interphase yeast showed direct communication between nuclear envelope, ER and segregated Golgi cisternae. A new class of constitutive conveyors, coated protein globules smaller than membrane vesicles, was shown to exist throughout the cell cycle. The function of Golgi-derived membrane vesicles was constrained to promotion of exocytosis in budding yeast. Some of the Golgi apparatus functions were detected in both these classes of exocytotic conveyors. Uptake (phagocytosis) of transport conveyors and lipoprotein condensates has been shown to deliver enzymes and secretory compounds into vacuoles. This simplified machinery of secretion, postulated for S. cerevisiae, does not include the Golgi cascade.
authors.affiliation: Institute of Microbiology, Academy of Sciences of the Czech Republic, Praha, Czech Republic.
authors.forename: J
authors.initials: J
authors.lastname: Vorísek
mesh_terms: D000818:Animals; D006023:Glycoproteins / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism* / Q000648:ultrastructure; D006651:Histocytochemistry; D016253:Microscopy, Immunoelectron; D012441:Saccharomyces cerevisiae / Q000378:metabolism* / Q000648:ultrastructure
chemical_list: D006023:Glycoproteins