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Significance Vital physiological processes—such as the cytotoxic immune response—require the coordinated action of the atypical fusion protein Syntaxin 11 (STX11) and the Sec/Munc protein Munc18-2 for releasing effector proteins housed in membrane-enclosed secretory granules. Human mutations in STX11 and Munc18-2 genes lead to severe immunodeficiency and hemostasis disorders. However it is still unclear how STX11, a lipid-anchored SNARE, and Munc18-2 mediate membrane fusion. By using an in vitro fusion assay, we found that STX11 mainly mediates lipid mixing when combined with human lymphocyte-interacting SNAREs. Remarkably, Munc18-2 induces association among these SNAREs and facilitates the transition from a hemifusion-like state to complete fusion. Our findings support a model in which SM proteins play a direct role in membrane merging.

SM protein Munc18-2 facilitates transition of Syntaxin 11-mediated lipid mixing to complete fusion for T-lymphocyte cytotoxicity