Dynamic transport of SNARE proteins in the Golgi apparatus

doi:10.1073/pnas.0507394102

Dynamic transport of SNARE proteins in the Golgi apparatus

^*Department of Cell Physiology and Metabolism, University of Geneva Medical School, 1211 Geneva 4, Switzerland; ^§Department of Physiology and Cellular Biophysics, Columbia University College of Physicians and Surgeons, 1150 St. Nicholas Avenue, New York, NY 10032; and ^†Memorial Sloan–Kettering Cancer Center, New York, NY 10021

Contributed by Lelio Orci, August 26, 2005

Abstract

Localization of a membrane protein in a subcellular compartment can be achieved by its retention in the compartment or by its continuous transport toward this compartment. Previous results have suggested that specific enzymes are localized in the Golgi apparatus at least in part by selective retention and exclusion from transport vesicles. However, the function of some Golgi SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins is not compatible with their exclusion from transport vesicles. To help understand the mechanism accounting for the localization of SNARE proteins in the Golgi apparatus, we analyzed their lateral distribution in the Golgi cisternae and their incorporation into transport vesicles. According to our results, all SNARE proteins are efficiently incorporated into transport vesicles, indicating that the localization of SNARE proteins in the Golgi apparatus is not based on a static retention mechanism. Detailed analysis suggested that incorporation into transport vesicles was more efficient for SNARE proteins restricted to the cis face of the Golgi as compared with SNAREs present at the trans face. Furthermore, overexpression of a cis-Golgi SNARE protein altered concomitantly its incorporation in transport vesicles and its intra-Golgi localization. These observations suggest that, contrary to resident Golgi enzymes, SNARE proteins are localized in the Golgi apparatus as the result of a dynamic transport equilibrium.

Footnotes

↵ ¶ To whom correspondence should be addressed. E-mail: lelio.orci{at}medecine.unige.ch.
↵ ‡ Present address: Toronto General Research Institute, 200 Elizabeth Street, Toronto, Canada M5G 2C4.
Abbreviations: SNARE, soluble N-ethylmaleimide-sensitive factor attachment protein receptor; v-SNARE, SNARE present on the vesicular membrane; t-SNARE, SNARE present on the target membrane; ER, endoplasmic reticulum; KDEL, Lys-Asp-Glu-Leu.