endobrevin

Endobrevin, also known as vesicle-associated membrane protein 8 (VAMP8), is a small integral membrane protein of the SNARE family. It is encoded by the VAMP8 gene in humans and is localized to late endosomes and lysosomes, where it participates in membrane fusion events. Endobrevin contains a single C-terminal transmembrane domain that anchors it to vesicular membranes and a cytosolic SNARE motif that engages in complex formation with partner SNAREs.

Role in trafficking and fusion is central to endobrevin’s function. It participates in the fusion of late endosomes with lysosomes and supports the maturation of endocytic compartments. Through SNARE complex assembly with target-membrane SNAREs such as syntaxin family members and Vti1b, endobrevin promotes vesicle fusion and content delivery within the endolysosomal system. In addition to endosome-lysosome fusion, endobrevin is implicated in related processes such as endocytosis, protein degradation pathways, and possibly autophagosome-lysosome fusion. Its expression pattern is broad, with notable presence in cells that rely on endosomal trafficking for antigen processing and degradation.

Clinical and research notes highlight that perturbations in endobrevin function can affect endolysosomal trafficking and related cellular activities. While not typically a primary disease gene, alterations in SNARE components like endobrevin can influence immune cell function and intracellular transport in experimental models. As part of the broader SNARE network, endobrevin remains a focus of study for understanding intracellular trafficking mechanisms and their implications for health and disease.