Syntaxin specificity of cytokinesis in Arabidopsis

Abstract

Syntaxins interact with other SNAREs (soluble NSF-attachment protein receptors) to form structurally related complexes1 that mediate membrane fusion in diverse intracellular trafficking pathways2-5. The original SNARE hypothesis6 postulated that each type of transport vesicle has its own distinct vesicle-SNARE that pairs up with a unique target-SNARE, or syntaxin, on the target membrane. However, recent evidence suggests that small G-proteins of the Rab family and their effectors mediate the initial contact between donor and acceptor membranes7, providing complementary specificity to SNARE pairing at a later step towards membrane fusion3-5. To assess the role of syntaxin specificity in membrane recognition requires a biological assay in which one syntaxin is replaced by other family members that do not normally function in that trafficking pathway. Here, we examine whether membrane fusion in Arabidopsis thaliana cytokinesis, which involves a plant-specific syntaxin, the cell-cycle-regulated KNOLLE (KN) protein8,9, can be mediated by other syntaxins if expressed under the control of KN cis-regulatory sequences. Only a non-essential syntaxin was targeted to the plane of cell division and sufficiently related to KN to perform its function, thus revealing syntaxin specificity of cytokinesis.