Golgi complex: Stacking the cisternae
نویسنده
چکیده
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 proteins and lipids by Golgi enzymes depends on vesicle transport, regardless of whether the secretory cargo actually moves through the stack by vesicle transport, or whether it moves by cisternal maturation as some believe. It is therefore assumed, though not proven, that stack formation increases processing efficiency by decreasing the distances through which vesicles have to be transported. Vesicles are most abundant at the highly fenestrated rims of the cisternae, while compact stacking is most evident at the cisternal cores. In vertebrates, continuities of cisternal membranes in the rim region serve to link adjacent Golgi stacks, forming a ribbon of stacked membranes. Remarkably, in these cells, the linked Golgi stack is completely disassembled and reassembled every cell division to allow accurate Golgi inheritance by the daughter cells. What are the molecular processes that underlie the stacking of the Golgi cisternae?
منابع مشابه
GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system.
We have identified a 55 kDa protein, named GRASP55 (Golgi reassembly stacking protein of 55 kDa), as a component of the Golgi stacking machinery. GRASP55 is homologous to GRASP65, an N-ethylmaleimide-sensitive membrane protein required for the stacking of Golgi cisternae in a cell-free system. GRASP65 exists in a complex with the vesicle docking protein receptor GM130 to which it binds directly...
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In vitro assays identified the Golgi peripheral protein GRASP65 as a Golgi stacking factor that links adjacent Golgi cisternae by forming mitotically regulated trans-oligomers. These conclusions, however, require further confirmation in the cell. In this study, we showed that the first 112 amino acids at the N-terminus (including the first PDZ domain, PDZ1) of the protein are sufficient for oli...
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عنوان ژورنال:
- Current Biology
دوره 9 شماره
صفحات -
تاریخ انتشار 1999