Brefeldin A, a drug that blocks secretion, prevents the assembly of non-clathrin-coated buds on Golgi cisternae
L Orcl, M Tagaya, M Amherdt, A Perrelet… - Cell, 1991 - cell.com
L Orcl, M Tagaya, M Amherdt, A Perrelet, JG Donaldson, J Lippincott-Schwartz, RD Klausner…
Cell, 1991•cell.comWe report that brefeldin A prevents the assembly of non-clathrintoated vesicles from Golgl
clsternae in a ceil-free system. This finding provldes a simple molecular explanation for the
primary effect of this remarkable compound in blocking constitutive secretion. We further
report that when coated vesicle assembly is blocked, extensive tubule networks form that
connect previously separate cisternae and stacks into a single topological unit, allowlng the
intermixing of contents of Golgl clsternae, presumably by lateral dlffuslon. Formation of the …
clsternae in a ceil-free system. This finding provldes a simple molecular explanation for the
primary effect of this remarkable compound in blocking constitutive secretion. We further
report that when coated vesicle assembly is blocked, extensive tubule networks form that
connect previously separate cisternae and stacks into a single topological unit, allowlng the
intermixing of contents of Golgl clsternae, presumably by lateral dlffuslon. Formation of the …
Summary
We report that brefeldin A prevents the assembly of non-clathrintoated vesicles from Golgl clsternae in a ceil-free system. This finding provldes a simple molecular explanation for the primary effect of this remarkable compound in blocking constitutive secretion. We further report that when coated vesicle assembly is blocked, extensive tubule networks form that connect previously separate cisternae and stacks into a single topological unit, allowlng the intermixing of contents of Golgl clsternae, presumably by lateral dlffuslon. Formation of the tubule networks requires ATP, cytosol, and the general fusion protein NSF. Tubule networks may be related to the membrane tubules mediating retrograde tmnsport In vlvo.
Brefeldin A (BFA) rapidly and reversibly blocks transport of secretory proteins to the Golgi apparatus, and also results in a dramatic resorption of most of the membrane of the Golgi into the endoplasmic reticulum (ER)(Misumi et al., 1988; Oda et al., 1987; Fujiwara et al., 1988; Lippinco&Schwartz et al., 1989). This resorption is most likely due to an ongoing process of retrograde transport (ie, Golgi toward ER) that predominates when anterograde (ie, ER toward Golgi toward cell surface) transport is blocked, as retrograde transport can also be observed in the absence of BFA when anterograde transport is selectively slowed by other means (Lippincott-Schwartz et al., 1990). Retrograde transport is likely to be mediated by
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