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MBC in Press, published online ahead of print October 18, 2006
Mol. Biol. Cell 10.1091/mbc.E06-06-0565

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Submitted on July 3, 2006
Revised on August 18, 2006
Accepted on October 5, 2006

The Golgi Apparatus Maintains Its Organization Independent of the Endoplasmic Reticulum

Matthew Y. Pecot and Vivek Malhotra

Department of Cell and Developmental Biology, University of California San Diego, La Jolla, CA 92093

Monitoring Editor: Francis Barr

Under artificial conditions Golgi enzymes have the capacity to rapidly accumulate in the Endoplasmic Reticulum (ER). These observations prompted the idea that Golgi enzymes constitutively recycle through the ER. We have tested this hypothesis under physiological conditions through use of a procedure that captures Golgi enzymes in the ER. In the presence of rapamycin, which induces a tight association between FKBP and FRAP, an FKBP-tagged Golgi enzyme can be trapped when it visits the ER by an ER retained protein fused to FRAP. We find that while FKBP-ERGIC-53 of the ER-Golgi Intermediate Compartment (ERGIC) rapidly cycles through the ER (30 min), FKBP-Golgi enzyme chimeras remain stably associated with Golgi membranes. We also demonstrate that Golgi dispersion upon nocodazole treatment mainly occurs through a mechanism that does not involve the recycling of Golgi membranes through the ER. Our findings suggest that the Golgi apparatus, as defined by its collection of resident enzymes, exists independent of the ER.

Address correspondence to: Vivek Malhotra (malhotra{at}biomail.ucsd.edu)




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