Recombinant Human VAMP4 protein (GST tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Vesicle-associated membrane protein 4 (VAMP4) mechanically participates in cellular processes linked to vesicle transport and fusion. Known alternatively as synaptobrevin-4 VAMP4 has a molecular mass of approximately 15 kDa. It localizes within the trans-Golgi network and endosomal compartments. VAMP4 associates with membranes during the trafficking of proteins and plays a significant role in regulating the fusion of vesicles with specific intracellular compartments.

Biological function summary

VAMP4 functions in mediating intracellular transport and fusion events and it is part of the SNARE complex. This complex facilitates the precise docking and fusion of vesicles a necessary process for maintaining cellular homeostasis. By partnering with other SNARE proteins VAMP4 controls the release and sorting of vesicular contents which is important for normal cell functions. Its action ensures that vesicles deliver their cargo to the correct location within the cell.

Pathways

The role of VAMP4 integrates into the broader network of intracellular trafficking pathways. It is especially significant in the Golgi-endosomal transport pathway and plays a coordinating role with other SNARE proteins like syntaxin and SNAP-23. Its interactions ensure vesicles reach their intended destinations within these pathways aiding in effective transport and fusion across cellular compartments.

VAMP4 connects with several neuropathological conditions such as Alzheimer’s disease and Parkinson’s disease. Alterations in VAMP4 expression or function can disturb vesicular transport and fusion contributing to the accumulation of misfolded proteins. Such imbalances often result in neuronal dysfunction. VAMP4 also interacts with proteins like alpha-synuclein which further links it to neurodegenerative disease pathways where improper vesicle traffic plays a significant role.