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URL: https://pubmed.ncbi.nlm.nih.gov/11739400/

⇱ Constructing a Golgi complex - PubMed

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Abstract

In this issue, Short et al. report the discovery of a protein named Golgin-45 that is located on the surface of the middle (or medial) cisternae of the Golgi complex. Depletion of this protein disrupts the Golgi complex and leads to the return of a resident, lumenal, medial Golgi enzyme to the endoplasmic reticulum. These findings suggest that Golgin-45 serves as a linchpin for the maintenance of Golgi complex structure, and offer hints as to the mechanisms by which the polarized Golgi complex is constructed.

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👁 Figure 1.
Figure 1.
The Golgi is comprised of minimally three distinct cisternae: cis, medial, and trans. Each cisternae houses different sets of resident Golgi enzymes that may be associated with one another within a given cisterna. One model for Golgi assembly would be that each cisterna has its own matrix: X, Y, and Z. If the medial matrix, Y, could bind both the cis matrix, X and the trans matrix, Z, but X and Z could not interact, a polarized structure could be generated. This model has a major flaw: a medial Golgi might bind two cis- or two trans-cisternae instead of one cis- and one trans-cisterna. Thus, the model shown includes medial Golgi matrix Y*, which can only bind the trans-Golgi. Y and Y* may represent different proteins or the same proteins, differently modified.

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