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Published 21 June 2004. doi:10.1083/jcb.200403120
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 165, Number 6, 781-788
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Actin dynamics coupled to clathrin-coated vesicle formation at the trans-Golgi network



Sebastien Carreno1, Åsa E. Engqvist-Goldstein1, Claire X. Zhang1, Kent L. McDonald2, and David G. Drubin1

1 Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720
2 Electron Microscope Laboratory, University of California, Berkeley, Berkeley, CA 94720

Address correspondence to David G. Drubin, 16 Barker Hall, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720-3202. Tel.: (510) 642-3692. Fax: (510) 643-0062. email: drubin{at}socrates.berkeley.edu


Abstract

In diverse species, actin assembly facilitates clathrin-coated vesicle (CCV) formation during endocytosis. This role might be an adaptation specific to the unique environment at the cell cortex, or it might be fundamental, facilitating CCV formation on different membranes. Proteins of the Sla2p/Hip1R family bind to actin and clathrin at endocytic sites in yeast and mammals. We hypothesized that Hip1R might also coordinate actin assembly with clathrin budding at the trans-Golgi network (TGN). Using deconvolution and time-lapse microscopy, we showed that Hip1R is present on CCVs emerging from the TGN. These vesicles contain the mannose 6-phosphate receptor involved in targeting proteins to the lysosome, and the actin nucleating Arp2/3 complex. Silencing of Hip1R expression by RNAi resulted in disruption of Golgi organization and accumulation of F-actin structures associated with CCVs on the TGN. Hip1R silencing and actin poisons slowed cathepsin D exit from the TGN. These studies establish roles for Hip1R and actin in CCV budding from the TGN for lysosome biogenesis.

Key Words: TGN; lysosomes; clathrin; actin; Hip1R

The online version of this article contains supplemental material.

Abbreviations used in this paper: CCV, clathrin-coated vesicle; CD-MPR, cation-dependent mannose 6-P receptor.


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