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« Previous Abstract"Longer commutes are associated with increased human exposure to tris(1,3-dichloro-2-propyl) phosphate"    Next AbstractAllele-specific suppression of a defective trans-Golgi network (TGN) localization signal in Kex2p identifies three genes involved in localization of TGN transmembrane proteins »

J Cell Biol


Title:Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae
Author(s):Redding K; Holcomb C; Fuller RS;
Address:"Department of Biochemistry, Stanford University School of Medicine, California 94305"
Journal Title:J Cell Biol
Year:1991
Volume:113
Issue:3
Page Number:527 - 538
DOI: 10.1083/jcb.113.3.527
ISSN/ISBN:0021-9525 (Print) 1540-8140 (Electronic) 0021-9525 (Linking)
Abstract:"The Kex2 protein of the yeast Saccharomyces cerevisiae is a membrane-bound, Ca2(+)-dependent serine protease that cleaves the precursors of the mating pheromone alpha-factor and the M1 killer toxin at pairs of basic residues during their transport through the secretory pathway. To begin to characterize the intracellular locus of Kex2-dependent proteolytic processing, we have examined the subcellular distribution of Kex2 protein in yeast by indirect immunofluorescence. Kex2 protein is located at multiple, discrete sites within wild-type yeast cells (average, 3.0 +/- 1.7/mother cell). Qualitatively similar fluorescence patterns are observed at elevated levels of expression, but no signal is found in cells lacking the KEX2 gene. Structures containing Kex2 protein are not concentrated at a perinuclear location, but are distributed throughout the cytoplasm at all phases of the cell cycle. Kex2-containing structures appear in the bud at an early, premitotic stage. Analysis of conditional secretory (sec) mutants demonstrates that Kex2 protein ordinarily progresses from the ER to the Golgi but is not incorporated into secretory vesicles, consistent with the proposed localization of Kex2 protein to the yeast Golgi complex"
Keywords:Cell Cycle Cytoplasmic Granules/enzymology Endoplasmic Reticulum/enzymology Fluorescent Antibody Technique Golgi Apparatus/*enzymology Mitosis Mutation *Proprotein Convertases Saccharomyces cerevisiae/cytology/*enzymology/genetics/ultrastructure *Saccharo;
Notes:"MedlineRedding, K Holcomb, C Fuller, R S eng GM39697/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. 1991/05/01 J Cell Biol. 1991 May; 113(3):527-38. doi: 10.1083/jcb.113.3.527"

 
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