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A correction to this article has been published: Audhya et al., J. Cell Biol. 178 (7) 1309
Published online
doi:10.1083/jcb.200701139
The Journal of Cell Biology, Vol. 178, No. 1, 43-56
The Rockefeller University Press, 0021-9525 $30.00
© Audhya et al.
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Article

A role for Rab5 in structuring the endoplasmic reticulum



Anjon Audhya, Arshad Desai, and Karen Oegema

Ludwig Institute for Cancer Research, Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093

Correspondence to Anjon Audhya: aaudhya{at}ucsd.edu; or Karen Oegema: koegema{at}ucsd.edu

The endoplasmic reticulum (ER) is a contiguous network of interconnected membrane sheets and tubules. The ER is differentiated into distinct domains, including the peripheral ER and nuclear envelope. Inhibition of two ER proteins, Rtn4a and DP1/NogoA, was previously shown to inhibit the formation of ER tubules in vitro. We show that the formation of ER tubules in vitro also requires a Rab family GTPase. Characterization of the 29 Caenorhabditis elegans Rab GTPases reveals that depletion of RAB-5 phenocopies the defects in peripheral ER structure that result from depletion of RET-1 and YOP-1, the C. elegans homologues of Rtn4a and DP1/NogoA. Perturbation of endocytosis by other means did not affect ER structure; the role of RAB-5 in ER morphology is thus independent of its well-studied requirement for endocytosis. RAB-5 and YOP-1/RET-1 also control the kinetics of nuclear envelope disassembly, which suggests an important role for the morphology of the peripheral ER in this process.

Abbreviations used in this paper: dsRNA, double-stranded RNA; GDI, GDP-dissociation inhibitor; GEF, guanine nucleotide exchange factor; INM, inner nuclear membrane.


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