Abstract
Several physiologically important proteins lack a classical secretory signal sequence, yet they are secreted from cells. To investigate the secretion mechanism of such proteins, a representative mammalian protein that is exported by a nonclassical mechanism, galectin-1, has been expressed in yeast. Galectin-1 is exported across the yeast plasma membrane, and this export does not require the classical secretory pathway nor the yeast multidrug resistance-like protein Ste6p, the transporter for the peptide a factor. A screen for components of the export machinery has identified genes that are involved in nonclassical export. These findings demonstrate a new pathway for protein export that is distinct from the classical secretory pathway in yeast.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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ATP-Binding Cassette Transporters / genetics
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ATP-Binding Cassette Transporters / metabolism
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Amino Acid Sequence
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Animals
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Biological Transport, Active / genetics
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DNA, Complementary / genetics
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DNA, Fungal / genetics
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Epitopes / genetics
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Escherichia coli / genetics
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Fungal Proteins / genetics
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Fungal Proteins / isolation & purification
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Fungal Proteins / metabolism*
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Galectin 1
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Genes, Fungal
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Glycoproteins*
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Hemagglutinins / genetics
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Hemagglutinins / immunology
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Hemagglutinins / metabolism*
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Hydrogen-Ion Concentration
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Molecular Sequence Data
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Recombinant Proteins / genetics
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Recombinant Proteins / immunology
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Recombinant Proteins / metabolism
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins*
Substances
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ATP-Binding Cassette Transporters
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DNA, Complementary
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DNA, Fungal
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Epitopes
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Fungal Proteins
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Galectin 1
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Glycoproteins
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Hemagglutinins
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Recombinant Proteins
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STE6 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
Associated data
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GENBANK/U41658
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GENBANK/U41659
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GENBANK/U52369