Sec24C is required for docking the prechylomicron transport vesicle with the Golgi
The rate-limiting step in the transit of dietary fat across the intestinal absorptive cell is its exit from the endoplasmic reticulum (ER) in a specialized ER-to-Golgi transport vesicle, the prechylomicron transport vesicle (PCTV). PCTV bud off from the ER membranes and have unique features; they ar...
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doaj-b8e65d8124314336a2f24ea9a48f0a772021-04-28T06:04:24ZengElsevierJournal of Lipid Research0022-22752010-05-0151510931100Sec24C is required for docking the prechylomicron transport vesicle with the GolgiShahzad Siddiqi0Shadab A. Siddiqi1Charles M. Mansbach, II2Division of Gastroenterology, Department of Medicine, University of Tennessee Health Science Center, Memphis, TNBurnett School of Biomedical Sciences, University of Central Florida, Orlando, FLTo whom correspondence should be addressed; Division of Gastroenterology, Department of Medicine, University of Tennessee Health Science Center, Memphis, TN; Veterans Affairs Medical Center, Memphis, TNThe rate-limiting step in the transit of dietary fat across the intestinal absorptive cell is its exit from the endoplasmic reticulum (ER) in a specialized ER-to-Golgi transport vesicle, the prechylomicron transport vesicle (PCTV). PCTV bud off from the ER membranes and have unique features; they are the largest ER-derived vesicles (average diameter 250 nm), do not require GTP and COPII proteins for their formation, and utilize VAMP7 as a v-N-ethylmaleimide sensitive factor attachment protein receptor (SNARE). However, PCTV require COPII proteins for their fusion with the Golgi, suggesting a role for them in Golgi target recognition. In support of this, PCTV contained each of the five COPII proteins when docked with the Golgi. When PCTV were fused with the Golgi, the COPII proteins were present in greatly diminished amounts, indicating they had cycled back to the cytosol. Immuno-depletion of Sec31 from the cytosol did not affect PCTV-Golgi docking, but depletion of Sec23 resulted in a 25% decrease. Immuno-depletion of Sec24C caused a nearly complete cessation of PCTV docking activity, but on the addition of recombinant Sec24C, docking activity was restored. We conclude that the COPII proteins are present at docking of PCTV with the Golgi and that Sec24C is required for this event. Sec23 plays a less important role.http://www.sciencedirect.com/science/article/pii/S002222752041065Xlipid absorptiontransport vesiclestriacylglycerolchylomicron |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Shahzad Siddiqi Shadab A. Siddiqi Charles M. Mansbach, II |
spellingShingle |
Shahzad Siddiqi Shadab A. Siddiqi Charles M. Mansbach, II Sec24C is required for docking the prechylomicron transport vesicle with the Golgi Journal of Lipid Research lipid absorption transport vesicles triacylglycerol chylomicron |
author_facet |
Shahzad Siddiqi Shadab A. Siddiqi Charles M. Mansbach, II |
author_sort |
Shahzad Siddiqi |
title |
Sec24C is required for docking the prechylomicron transport vesicle with the Golgi |
title_short |
Sec24C is required for docking the prechylomicron transport vesicle with the Golgi |
title_full |
Sec24C is required for docking the prechylomicron transport vesicle with the Golgi |
title_fullStr |
Sec24C is required for docking the prechylomicron transport vesicle with the Golgi |
title_full_unstemmed |
Sec24C is required for docking the prechylomicron transport vesicle with the Golgi |
title_sort |
sec24c is required for docking the prechylomicron transport vesicle with the golgi |
publisher |
Elsevier |
series |
Journal of Lipid Research |
issn |
0022-2275 |
publishDate |
2010-05-01 |
description |
The rate-limiting step in the transit of dietary fat across the intestinal absorptive cell is its exit from the endoplasmic reticulum (ER) in a specialized ER-to-Golgi transport vesicle, the prechylomicron transport vesicle (PCTV). PCTV bud off from the ER membranes and have unique features; they are the largest ER-derived vesicles (average diameter 250 nm), do not require GTP and COPII proteins for their formation, and utilize VAMP7 as a v-N-ethylmaleimide sensitive factor attachment protein receptor (SNARE). However, PCTV require COPII proteins for their fusion with the Golgi, suggesting a role for them in Golgi target recognition. In support of this, PCTV contained each of the five COPII proteins when docked with the Golgi. When PCTV were fused with the Golgi, the COPII proteins were present in greatly diminished amounts, indicating they had cycled back to the cytosol. Immuno-depletion of Sec31 from the cytosol did not affect PCTV-Golgi docking, but depletion of Sec23 resulted in a 25% decrease. Immuno-depletion of Sec24C caused a nearly complete cessation of PCTV docking activity, but on the addition of recombinant Sec24C, docking activity was restored. We conclude that the COPII proteins are present at docking of PCTV with the Golgi and that Sec24C is required for this event. Sec23 plays a less important role. |
topic |
lipid absorption transport vesicles triacylglycerol chylomicron |
url |
http://www.sciencedirect.com/science/article/pii/S002222752041065X |
work_keys_str_mv |
AT shahzadsiddiqi sec24cisrequiredfordockingtheprechylomicrontransportvesiclewiththegolgi AT shadabasiddiqi sec24cisrequiredfordockingtheprechylomicrontransportvesiclewiththegolgi AT charlesmmansbachii sec24cisrequiredfordockingtheprechylomicrontransportvesiclewiththegolgi |
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