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Originally published as MBC in Press, 10.1091/mbc.E06-06-0565 on October 18, 2006

Vol. 17, Issue 12, 5372-5380, December 2006

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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

Submitted July 3, 2006; Revised August 18, 2006; Accepted October 5, 2006
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 (FK506-binding protein) and FRAP (FKBP-rapamycin–associated protein), an FKBP-tagged Golgi enzyme can be trapped when it visits the ER by an ER-retained protein fused to FRAP. We find that although 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.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-06-0565) on October 18, 2006.

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




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