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First published online January 21, 2009


Journal of Cell Science 122, 302e (2009)
© The Company of Biologists Limited
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In this issue

(Retrograde) traffic duty for EHD3


Figure 1

Extracellular contents, fluids and cell-surface proteins are internalised by cells via a process known as endocytosis. Trafficking through the endocytic pathway is regulated by a number of proteins, including the recently implicated C-terminal Eps15-homology domain-containing (EHD) family. Naava Naslavsky, Steve Caplan and colleagues previously showed that EHD3 regulates early-endosome-to-recycling-endosome transport, and now, on page 389, they examine whether EHD3 is also involved in the regulation of endosome-to-Golgi retrograde transport. The authors show that knockdown of EHD3, or its interacting partner rabenosyn-5, by siRNA prevents the transport of the internalised retrograde cargo protein Shiga toxin B subunit (STxB) to the Golgi, and causes alterations in Golgi morphology. Depletion of EHD3 also causes accumulation of the mannose 6-phosphate receptor upstream of the Golgi and prevents cathepsin D from exiting the Golgi; by contrast, transport of the secretory membrane protein VSVG from the Golgi to the plasma membrane is not affected. Thus, EHD3 has a new role as a key regulator that modulates traffic between endosomes and the Golgi. The authors suggest that future studies are needed to dissect the roles that individual EHD proteins carry out in trafficking from endosomes to the Golgi.


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Related articles in JCS:

EHD3 regulates early-endosome-to-Golgi transport and preserves Golgi morphology
Naava Naslavsky, Jenna McKenzie, Nihal Altan-Bonnet, David Sheff, and Steve Caplan
JCS 2009 122: 389-400. [Abstract] [Full Text]  




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