The Di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding.

Abstract

Heterotetrameric adaptor complexes and SNAREs play key roles in the specificity of membrane budding and fusion. Here we test the hypothesis that vesicle budding and membrane fusion are coupled by the interaction of these molecules. We investigate the role of the di-leucine motif of vesicle-associated membrane protein 4 (VAMP4) in adaptor binding and localization of VAMP4. Mutation of the di-leucine motif inhibits AP-1 binding in vitro and affects the steady state distribution of VAMP4 in vivo.

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@article{Peden2001TheDM, title={The Di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding.}, author={Andrew A Peden and Grace Y Park and Richard H. Scheller}, journal={The Journal of biological chemistry}, year={2001}, volume={276 52}, pages={49183-7} }