Abstract
The Golgi apparatus is partitioned during mitosis in animal cells by a process of fragmentation, dispersal, and reassembly in each daughter cell. We fractionated the Golgi apparatus in vivo using the drug brefeldin A or a dominant-negative mutant of the Sar1p protein. After these treatments, Golgi enzymes moved back to the endoplasmic reticulum, leaving behind a matrix of Golgi structural proteins. Under these conditions, cells still entered and exited mitosis normally, and their Golgi matrix partitioned in a manner very similar to that of the complete organelle. Thus, the matrix may be the partitioning unit of the Golgi apparatus and may carry the Golgi enzyme-containing membranes into the daughter cells.
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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Anaphase
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Animals
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Autoantigens
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Brefeldin A / pharmacology
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Cell Line
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Endoplasmic Reticulum / enzymology
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Golgi Apparatus / metabolism*
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Golgi Apparatus / ultrastructure
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Golgi Matrix Proteins
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HeLa Cells
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Humans
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Interphase
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Intracellular Membranes / metabolism
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Intracellular Membranes / ultrastructure
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Mannosidases / metabolism
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Membrane Proteins / metabolism
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Metaphase
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Microscopy, Electron
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Microscopy, Fluorescence
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Mitosis*
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Monomeric GTP-Binding Proteins / pharmacology
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N-Acetylglucosaminyltransferases / metabolism
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Protein Disulfide-Isomerases / metabolism
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Rats
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Saccharomyces cerevisiae Proteins*
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Telophase
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Vesicular Transport Proteins
Substances
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Autoantigens
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GORASP1 protein, human
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Golgi Matrix Proteins
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Golgin subfamily A member 2
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Gorasp1 protein, rat
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Membrane Proteins
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Saccharomyces cerevisiae Proteins
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Vesicular Transport Proteins
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Brefeldin A
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N-Acetylglucosaminyltransferases
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alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase I
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Mannosidases
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mannosyl-oligosaccharide 1,3 - 1,6-alpha-mannosidase
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Monomeric GTP-Binding Proteins
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SAR1 protein, S cerevisiae
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Protein Disulfide-Isomerases