| | |  | | | | Record from Web of Science® | | | | | | |
| Isolation of functional Golgi-derived vesicles with a possible role in retrograde transport |
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| Author(s): Love HD, Lin CC, Short CS, Ostermann J |
| Source: JOURNAL OF CELL BIOLOGY Volume: 140 Issue: 3 Pages: 541-551 Published: FEB 9 1998 |
| Times Cited: 59 References: 43 |
| Abstract: 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. |
| Document Type: Article |
| Language: English |
| Reprint Address: Ostermann, J (reprint author), Vanderbilt Univ, Sch Med, Dept Biochem, 221 Kirkland Hall, Nashville, TN 37232 USA |
Addresses:
1. Vanderbilt Univ, Sch Med, Dept Biochem, Nashville, TN 37232 USA |
| Publisher: ROCKEFELLER UNIV PRESS, 1114 FIRST AVE, 4TH FL, NEW YORK, NY 10021 USA |
| Subject Category: Cell Biology |
| IDS Number: YX299 |
| ISSN: 0021-9525 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |