Abstract
The docking of transport vesicles with their target membrane is thought to be mediated by p115. We show here that GM130, a cis-Golgi matrix protein, interacts specifically with p115 and so could provide a membrane docking site. Deletion analysis showed that the N-terminus binds to p115, whereas the C-terminus binds to Golgi membranes. Mitotic phosphorylation of GM130 or a peptide derived from the N-terminus prevented binding to p115. The peptide also inhibited the NSF- but not the p97-dependent reassembly of Golgi cisternae from mitotic fragments, unless it was mitotically phosphorylated. Together, these data provide a molecular explanation for the COPI-mediated fragmentation of the Golgi apparatus at the onset of mitosis.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Autoantigens
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Carrier Proteins / metabolism*
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Cell Line / physiology
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Golgi Apparatus / chemistry
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Golgi Apparatus / metabolism*
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Golgi Matrix Proteins
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Kidney / cytology
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Liver / chemistry
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Membrane Proteins / chemistry
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Mitosis / physiology*
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Molecular Sequence Data
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Octoxynol
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Peptide Fragments / metabolism
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Protein Binding / physiology
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Protein Structure, Tertiary
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Rats
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Salts
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Vesicular Transport Proteins*
Substances
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Autoantigens
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Carrier Proteins
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Golgi Matrix Proteins
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Golgin subfamily A member 2
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Membrane Proteins
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Peptide Fragments
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Salts
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Vesicular Transport Proteins
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vesicular transport factor p115
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Octoxynol