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Vol. 15, Issue 4, 1506-1518, April 2004

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Countercurrent Distribution of Two Distinct SNARE Complexes Mediating Transport within the Golgi Stack

Allen Volchuk ^*, Mariella Ravazzola , Alain Perrelet , William S. Eng ^*, Maurizio Di Liberto ^*, Oleg Varlamov ^*, Masayoshi Fukasawa ^*, Thomas Engel ^*, Thomas H. Söllner ^*, James E. Rothman ^* , and Lelio Orci 

Department of Morphology, University of Geneva Medical School, Geneva, Switzerland; ^* Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021

Submitted August 27, 2003; Revised October 22, 2003; Accepted October 22, 2003
Monitoring Editor: Randy Schekman

Genetic and biochemical evidence has established that a SNARE complex consisting of syntaxin 5 (Sed5)-mYkt6 (Ykt6)-GOS28 (Gos1)-GS15 (Sft1) is required for transport of proteins across the Golgi stack in animals (yeast). We have utilized quantitative immunogold labeling to establish the cis-trans distribution of the v-SNARE GS15 and the t-SNARE subunits GOS28 and syntaxin 5. Whereas the distribution of the t-SNARE is nearly even across the Golgi stack from the cis to the trans side, the v-SNARE GS15 is present in a gradient of increasing concentration toward the trans face of the stack. This contrasts with a second distinct SNARE complex, also required for intra-Golgi transport, consisting of syntaxin 5 (Sed5)-membrin (Bos1)-ERS24 (Sec22)-rBet1 (Bet1), whose v-(rBet1) and t-SNARE subunits (membrin and ERS24), progressively decrease in concentration toward the trans face. Transport within the stack therefore appears to utilize countercurrent gradients of two Golgi SNAREpins and may involve a mechanism akin to homotypic fusion.

Abbreviations used: CHO, Chinese hamster ovary; CGN, cis-Golgi network; IC, intermediate compartment; GFP, green fluorescent protein; NRK, normal rat kidney cells; SNARE, soluble N-ethylmaleimide-sensitive factor attachment protein receptor; TGN, trans-Golgi network; VSV, vesicular stomatitis virus; VSV-G, vesicular stomatitis virus glycoprotein.

Corresponding author. E-mail address: j-rothman{at}ski.mskcc.org.

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