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Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
Abstract
Cells of a Saccharomyces cerevisiae mutant that is temperature-sensitive for secretion and cell surface growth become dense during incubation at the non-permissive temperature (37 degrees C). This property allows the selection of additional secretory mutants by sedimentation of mutagenized cells on a Ludox density gradient. Colonies derived from dense cells are screened for conditional growth and secretion of invertase and acid phosphatase. The sec mutant strains that accumulate an abnormally large intracellular pool of invertase at 37 degrees C (188 mutant clones) fall into 23 complementation groups, and the distribution of mutant alleles suggests that more complementation groups could be found. Bud emergence and incorporation of a plasma membrane sulfate permease activity stop quickly after a shift to 37 degrees C. Many of the mutants are thermoreversible; upon return to the permissive temperature (25 degrees C) the accumulated invertase is secreted. Electron microscopy of sec mutant cells reveals, with one exception, the temperature-dependent accumulation of membrane-enclosed secretory organelles. We suggest that these structures represent intermediates in a pathway in which secretion and plasma membrane assembly are colinear.
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The exocyst is recruited to vesicle membranes by small GTPases and mediates the tethering of these vesicles to target membranes.
“The exocyst is recruited to vesicle membranes by small GTPases and mediates the tethering of these vesicles to target membranes.”
From Genome-scale CRISPR screening for modifiers of cellular LDL uptake (2021) · cites this paper as [21]
The exocyst is an octameric protein complex that was originally identified for its role in vesicular trafficking in budding yeast.
“an octameric protein complex that was originally identified for its role in vesicular trafficking in budding yeast[20,21]”
From Genome-scale CRISPR screening for modifiers of cellular LDL uptake (2021) · cites this paper as [21]
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Research works printed but not linked: 24
- Bassford, 1979, Escherichia coli mutants accumulating the precursor of a secreted protein in the cytoplasm, Nature, 277, 538, 10.1038/277538a0 · DOI
- Bassford, 1979, Use of gene fusion to study secretion of maltose-binding protein into Escherichia coli periplasm, J. Bacteriol., 139, 19, 10.1128/JB.139.1.19-31.1979 · DOI
- Breton, 1977, Sulfate uptake in Saccharomyces cerevisiae: biochemical and genetic study, J. Bacteriol., 132, 224, 10.1128/JB.132.1.224-232.1977 · DOI
- Byers, 1975, Behavior of spindles and spindle plaques in the cell cycle and conjugation of Saccharomyces cerevisiae, J. Bacteriol., 124, 511, 10.1128/JB.124.1.511-523.1975 · DOI
- Dodyk, 1964, Factors influencing the appearance of invertase in Saccharomyces cerevisiae, Arch. Biochem. Biophys., 104, 478, 10.1016/0003-9861(64)90492-8 · DOI
- Field, 1980, Localized secretion of acid phosphatase reflects the pattern of cell surface growth in Saccharomyces cerevisiae, J. Cell Biol., 86, 10.1083/jcb.86.1.123 · DOI
- Fincham, 1977, Allelic complementation reconsidered, Carlsberg Res. Commun., 42, 421, 10.1007/BF02906278 · DOI
- Goldstein, 1975, β-D-Fructofuranoside fructohydrolase from yeast, Meth. Enzymol., 42, 504, 10.1016/0076-6879(75)42159-0 · DOI
- Hansche, 1978, Gene duplication in Saccharomyces cerevisiae, Genetics, 88, 673, 10.1093/genetics/88.4.673 · DOI
- Henry, 1977, Growth and metabolism of inositol-starved Saccharomyces cerevisiae, J. Bacteriol., 130, 472, 10.1128/JB.130.1.472-484.1977 · DOI
- Katz, 1977, Membrane assembly: synthesis and intracellular processing of the vesicular stomatitis viral glycoprotein, J. Supramol. Structure, 7, 353, 10.1002/jss.400070308 · DOI
- Lehle, 1979, Carbohydrate structure of yeast invertase, J. Biol. Chem., 254, 12209, 10.1016/S0021-9258(19)86451-7 · DOI
- Marriot, 1979, Localization of dolichyl phosphate- and pyrophosphate-dependent glycosyl transfer reactions in Saccharomyces cerevisiae, J. Bacteriol., 139, 565
- Moor, 1967, Endoplasmic reticulum as the initiator of bud formation in yeast (Saccharomyces cerevisiae), Arch. Mikrobiol., 57, 135, 10.1007/BF00408697 · DOI
- Palade, 1975, Intracellular aspects of the process of protein synthesis, Science, 189, 347, 10.1126/science.1096303 · DOI
- Parodi, 1979, Biosynthesis of yeast mannoproteins: synthesis of mannan outer chain and of dolichol derivatives, J. Biol. Chem., 254, 8343, 10.1016/S0021-9258(19)86896-5 · DOI
- Price, 1977, On the purification of the silica sol Ludox AM, Anal. Biochem., 82, 243, 10.1016/0003-2697(77)90155-5 · DOI
- Raschke, 1973, Genetic control of yeast mannan structure, J. Biol. Chem., 248, 4660, 10.1016/S0021-9258(19)43714-9 · DOI
- Rubin, 1973, The nucleotide sequence of Saccharomyces cerevisiae 5.8S ribosomal ribonucleic acid, J. Biol. Chem., 248, 3860, 10.1016/S0021-9258(19)43814-3 · DOI
- Scott, 1980, Lyticase: endoglucanase and protease activities that act together in yeast cell lysis, J. Bacteriol., 142, 414, 10.1128/JB.142.2.414-423.1980 · DOI
- Tkacz, 1972, Wall replication in Saccharomyces species: use of fluorescein-conjugated concanavalin A to reveal the site of mannan insertion, J. Gen. Microbiol., 72, 243, 10.1099/00221287-72-2-243 · DOI
- Tkacz, 1973, Surface distribution of invertase on growing Saccharomyces cells, J. Bacteriol., 113, 1073, 10.1128/JB.113.2.1073-1075.1973 · DOI
- van Rijn, 1975, Localization of acid phosphatase in protoplasts from Saccharomyces cerevisiae, J. Bacteriol., 123, 1144, 10.1128/JB.123.3.1144-1149.1975 · DOI
- Wickerham, 1946, A critical evaluation of the nitrogen assimilation tests commonly used in the classification of yeasts, J. Bacteriol., 52, 293, 10.1128/JB.52.3.293-301.1946 · DOI
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Metadata
- Authors
- Novick, P., Field, C., & Schekman, R.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1980-08
- Volume
- 21
- Issue
- 1
- Pages
- 205-215
- ISSN
- 0092-8674
- Cited by
- 1,449
- References
- 0
- Language
- en
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