Isolation of Functional Golgi-Derived Vesicles with a Possible Role in Retrograde Transport

Secretory proteins enter the Golgi apparatus when transport vesicles fuse with the cis-side and exit in transport vesicles budding from the trans-side. Resident Golgi enzymes that have been transported in the cis-to-trans direction with the secretory flow must be recycled constantly by retrograde tr...

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Bibliographic Details
Published in:The Journal of cell biology 1998-02, Vol.140 (3), p.541-551
Main Authors: Love, Harold D., Lin, Chung-Chih, Short, Craig S., Ostermann, Joachim
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - metabolism
Animals
Biological Transport
Cell Fractionation
Cell membranes
Cells
Cellular biology
Centrifugation
CHO Cells
Coated Vesicles - metabolism
Coatomer Protein
Cricetinae
Cytosol
Cytosol - metabolism
Enzymes
Golgi apparatus
Golgi Apparatus - enzymology
Golgi Apparatus - metabolism
Ice
Intracellular Membranes - enzymology
Intracellular Membranes - metabolism
Membrane Glycoproteins
Membrane Proteins - metabolism
N-Acetylglucosaminyltransferases - metabolism
Organelles - enzymology
Organelles - metabolism
P branes
Proteins
Proteins - metabolism
String theory
Transport vesicles
Viral Envelope Proteins - metabolism
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Summary:Secretory proteins enter the Golgi apparatus when transport vesicles fuse with the cis-side and exit in transport vesicles budding from the trans-side. Resident Golgi enzymes that have been transported in the cis-to-trans direction with the secretory flow must be recycled constantly by retrograde transport in the opposite direction. In this study, we describe the functional characterization of Golgi-derived transport vesicles that were isolated from tissue culture cells. We found that under the steady-state conditions of a living cell, a fraction of resident Golgi enzymes was found in vesicles that could be separated from cisternal membranes. These vesicles appeared to be depleted of secretory cargo. They were capable of binding to and fusion with isolated Golgi membranes, and after fusion their enzymatic contents most efficiently processed cargo that had just entered the Golgi apparatus. Those results indicate a possible role for these structures in recycling of Golgi enzymes in the Golgi stack.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.140.3.541