Golgi complex: Stacking the cisternae

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Golgi complex: Stacking the cisternae

Stacks of disc-shaped cisternal membranes are a defining feature of the Golgi complex. Secretory products move through the stack from the ‘cis’ cisternae — which receives cargo from the endoplasmic reticulum (ER) — to the ‘trans’ cisternae on the opposite side, and most Golgilocalized proteins are targeted to the cis, medial or trans subcompartments. The efficient processing of secretory protei...

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GRASP65, a Protein Involved in the Stacking of Golgi Cisternae

NEM prevents mitotic reassembly of Golgi cisternae into stacked structures. The major target of NEM is a 65 kDa protein conserved from yeast to mammals. Antibodies to this protein and a recombinant form of it block cisternal stacking in a cell-free system, justifying its designation as a Golgi ReAssembly Stacking Protein (GRASP65). One of the two minor targets of NEM is GM130, previously implic...

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Stacking of Golgi cisternae in Schizosaccharomyces pombe requires intact microtubules.

Fission yeast was treated with the anti-microtubule agent, thiabendazole. Cytoplasmic microtubules broke down with a half-time of less than 10 minutes followed closely by the unstacking of Golgi cisternae. The final product appeared to be single Golgi cisternae. No other organelle seemed to be affected by this treatment, which was completely reversible. The nda3 mutant strain has an altered bet...

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Compartmentation of the Golgi complex: brefeldin-A distinguishes trans- Golgi cisternae from the trans-Golgi network

The Golgi complex is composed of at least four distinct compartments, termed the cis-, medial, and trans-Golgi cisternae and the trans-Golgi network (TGN). It has recently been reported that the organization of the Golgi complex is disrupted in cells treated with the fungal metabolite, brefeldin-A. Under these conditions, it was shown that resident enzymes of the cis-, medial, and trans-Golgi r...

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Intranuclear Cisternae Resembling Structures of the Golgi Complex

The presence of cytoplasmic structures, apparently inside the nuclei of neoplastic cells, has been observed repeatedly in the electron microscope (1). These structures, designated "nuclear pseudoinclusions" (1), are the result of cross-sections of cytoplasmic invaginations of the nuclear membrane. Their extranuclear origin is evident, since these structures are surrounded by a well defined, dou...

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ژورنال

عنوان ژورنال: Current Biology

سال: 1999

ISSN: 0960-9822

DOI: 10.1016/s0960-9822(00)80077-9