Abstract
Intracellular trafficking is essential for cell structure and function. In order to perform key tasks such as phagocytosis, secretion or migration, cells must coordinate their intracellular trafficking, and cytoskeleton dynamics. This relies on certain classes of proteins endowed with specialized and conserved domains that bridge membranes with effector proteins. Of particular interest are proteins capable of interacting with membrane subdomains enriched in specific phosphatidylinositol lipids, tightly regulated by various kinases and phosphatases. Here, we focus on the poorly studied RUFY family of adaptor proteins, characterized by a RUN domain, which interacts with small GTP-binding proteins, and a FYVE domain, involved in the recognition of phosphatidylinositol 3-phosphate. We report recent findings on this protein family that regulates endosomal trafficking, cell migration and upon dysfunction, can lead to severe pathology at the organismal level.
Highlights
The organization of cells into multiple membranous compartments with specific biochemical functions requires complex intracellular traffic and sorting of lipids and proteins, to transport them from their sites of synthesis to their functional destination
FYVE And Coiled-Coil Domain Autophagy Adaptor 1 (FYCO1) can indirectly associated with cell invasion (Pedersen et al, 2020). They have been poorly characterized to date, RUFY proteins play a central role in cellular homeostasis by regulating endocytosis, autophagy and coordinating organelle transport with signal transduction cascades
It is important to note that RUFY proteins provide a regulatory link between cytoskeletal dynamics and membrane trafficking
Summary
The organization of cells into multiple membranous compartments with specific biochemical functions requires complex intracellular traffic and sorting of lipids and proteins, to transport them from their sites of synthesis to their functional destination. As well as promoting endosomal fusion through their binding to Rab or Rap GTPases
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