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Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ER

Open access
Lippincott-Schwartz, Jennifer, Yuan, Lydia C., Bonifacino, Juan S., Klausner, Richard D.·1989·Cell

Abstract

In cells treated with brefeldin A (BFA), movement of newly synthesized membrane proteins from the endoplasmic reticulum (ER) to the Golgi apparatus was blocked. Surprisingly, the glycoproteins retained in the ER were rapidly processed by cis/medial Golgi enzymes but not by trans Golgi enzymes. An explanation for these observations was provided from morphological studies at both the light and electron microscopic levels using markers for the cis/medial and trans Golgi. They revealed a rapid and dramatic redistribution to the ER of components of the cis/medial but not the trans Golgi in response to treatment with BFA. Upon removal of BFA, the morphology of the Golgi apparatus was rapidly reestablished and proteins normally transported out of the ER were efficiently and rapidly sorted to their final destinations. These results suggest that BFA disrupts a dynamic membrane-recycling pathway between the ER and cis/medial Golgi, effectively blocking membrane transport out of but not back to the ER.

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Metadata

Authors
Lippincott-Schwartz, J., Yuan, L. C., Bonifacino, J. S., & Klausner, R. D.
Venue
Cell
Publisher
Elsevier BV
Published
1989-03
Volume
56
Issue
5
Pages
801-813
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2107312415
Cited by
1,687
References
0
FWCI
35.41
Type
journal article
Language
en
Open access
green

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