Abstract
Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) are required for the binding of N-ethylmaleimide-sensitive fusion protein (NSF) to Golgi membranes and are, therefore, required for intra-Golgi transport. We report the existence of distinct alpha/beta-SNAP and gamma-SNAP-binding sites in Golgi membranes that appear to be part of the same receptor complex. Cross-linking studies with alpha-SNAP demonstrate that an integral membrane protein of between 30-40 kDa is the alpha-SNAP binding component of the multi-SNAP receptor complex. These data suggest that SNAPs function by independently binding to a multi-SNAP membrane-receptor complex, thereby activating them to serve as adaptors for the targeting of NSF.
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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Amino Acid Sequence
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Animals
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Binding Sites
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Carrier Proteins / metabolism*
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Cross-Linking Reagents
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Electrophoresis, Polyacrylamide Gel
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Ethylmaleimide / pharmacology
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Golgi Apparatus / metabolism*
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Intracellular Membranes / metabolism
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Liver / metabolism
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Membrane Proteins / metabolism*
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Molecular Sequence Data
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N-Ethylmaleimide-Sensitive Proteins
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Rats
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Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
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Solutions
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Vesicular Transport Proteins*
Substances
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Carrier Proteins
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Cross-Linking Reagents
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Membrane Proteins
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Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
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Solutions
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Vesicular Transport Proteins
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N-Ethylmaleimide-Sensitive Proteins
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Nsf protein, rat
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Ethylmaleimide