Abstract
Scp160p is an RNA-binding protein containing 14 tandemly repeated heterogenous nuclear ribonucleoprotein K-homology domains, which are implicated in RNA binding. Scp160p interacts with free and membrane-bound polysomes that are dependent upon the presence of mRNA. Despite its presence on cytosolic polysomes, Scp160p is predominantly localized to the endoplasmic reticulum (ER). Accumulation of Scp160p-ribosome complexes at the ER requires the function of microtubules but is independent of the actin cytoskeleton. We propose that the multi-K-homology-domain protein Scp160p functions as an RNA binding platform, interacting with polysomes that are transported to the ER.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actins / metabolism
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Cell Fractionation
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Cell Membrane / drug effects
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Cell Membrane / metabolism
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Cell Membrane / ultrastructure
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Cytoskeleton / metabolism
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Cytoskeleton / ultrastructure
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Cytosol / metabolism
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Endoplasmic Reticulum / metabolism*
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Endoplasmic Reticulum / ultrastructure
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Fungal Proteins / metabolism
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Polymerase Chain Reaction
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Polyribosomes / metabolism*
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Polyribosomes / ultrastructure
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Protein Transport
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Puromycin / pharmacology
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RNA, Messenger / metabolism
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RNA-Binding Proteins
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Recombinant Fusion Proteins / metabolism
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Recombinant Proteins / metabolism
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Ribosomes / metabolism*
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Ribosomes / ultrastructure
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae / ultrastructure
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Saccharomyces cerevisiae Proteins*
Substances
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Actins
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Fungal Proteins
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Membrane Proteins
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Nuclear Proteins
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RNA, Messenger
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RNA-Binding Proteins
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Recombinant Fusion Proteins
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Recombinant Proteins
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SCP160 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Puromycin