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Review
. 2011 Oct 1;3(10):a005249.
doi: 10.1101/cshperspect.a005249.

Organization of SNAREs within the Golgi stack

Jörg Malsam  1 , Thomas H Söllner
Affiliations
Review

Organization of SNAREs within the Golgi stack

Jörg Malsam et al. Cold Spring Harb Perspect Biol. .

Abstract

Antero- and retrograde cargo transport through the Golgi requires a series of membrane fusion events. Fusion occurs at the cis- and trans-side and along the rims of the Golgi stack. Four functional SNARE complexes have been identified mediating lipid bilayer merger in the Golgi. Their function is tightly controlled by a series of reactions involving vesicle tethering and SM proteins. This network of protein interactions spatially and temporally determines the specificity of transport vesicle targeting and fusion within the Golgi.

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Figures

Figure 1.
Figure 1.
Structural organization of the SNARE four-helix bundle and SNARE motifs of ER and Golgi SNAREs. (A) Skeleton diagram of the synaptic SNARE four-helix bundle showing interacting layers (image is modified from Fasshauer et al. [1998] and reprinted, with permission, from the National Academy of Sciences ©1998). (B) SNARE motifs and membrane anchors of human SNAREs involved in ER and Golgi transport were aligned using the MULTALIN program (Corpet 1988). Interacting layers are shown in gray; amino acids in “0” layer and trans-membrane regions are highlighted in color. Ykt6 contains a CAXX box, which is farnesylated and palmitoylated. The Qa-, Qb-, Qc-, and R-SNARE classification is shown and SNAREs are listed according to their position in the secretory pathway: SEC20 (NP_053583.2), USE1 (NP_060937.1), BET1 (NP_005859.1), GS15 (AFF37877.1), syntaxin 6 (syx6) (CAA05177.1), syntaxin 10 (syx10) (AAC05087.1), SEC22b (NP_004883.2), YKT6 (NP_006546.1), VAMP3 (NP_004772.1), VAMP4 (NP_003753.2), syntaxin 18 (BAA95213.1), syntaxin 5 (AAC71078.1), syntaxin 16 (syx16) (AAC05647.1).
Figure 2.
Figure 2.
The localization and assignment of SNAREs and tethers to distinct membrane-trafficking steps at the Golgi of mammals and yeast. Four different sets, each containing one member of Qa-, Qb-, Qc-, and R-SNAREs mediate delivery to and transport within the Golgi. According to a morphological and quantitative analysis, the local distribution of some SNAREs involved in intra-Golgi transport is displayed. Tethering components are highlighted in gray. (ER: endoplasmic reticulum, IC: intermediate compartment, TGN: trans-Golgi network.)
Figure 3.
Figure 3.
Basic machinery controlling membrane fusion and SNARE recycling. SNAREs and tethers are recruited by vesicle coat components for uptake into a budding vesicle. The initial interaction of a vesicle with its target membrane is mediated by tethering proteins and a small Rab GTPase. Components of the tethering machinery trigger the formation of t-SNARE complexes, which assemble with their cognate v-SNAREs, resulting in the formation of SNAREpins. These events involve SM proteins and finally culminate in membrane fusion, which results in cis-v/t-SNARE complexes. In the presence of SNAPs, ATP-hydrolysis by NSF segregates v- and t-SNAREs for another round of fusion.
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