Function and Interactions of the Ysc84/SH3yl1 Family of Actin- and Lipid-Binding Proteins
January 2015
in “
Biochemical Society Transactions
”
actin filament membrane interactions cell motility endocytosis actin-related proteins plasma membrane endocytic invagination cell migration actin-binding YAB/SYLF domain SH3 domain actin polymerization Las17/WASP liposomes phosphoinositides actin cell movement cell membrane actin proteins cell surface actin-binding domain actin assembly Las17 lipid vesicles phospholipids
TLDR The Ysc84/SH3yl1 protein family is important for cell movement and the process of taking in materials by interacting with actin and cell membranes.
The document reviews the Ysc84/SH3yl1 family of proteins, highlighting their role in actin filament regulation and membrane interactions, which are crucial for cell motility and endocytosis. Ysc84 in yeast and SH3yl1 in mammalian cells interact with actin-related proteins and are involved in forming actin structures at the plasma membrane. Deletion or depletion of these proteins impairs endocytic invagination and cell migration, respectively. The proteins share a conserved domain structure, including an actin-binding YAB/SYLF domain and an SH3 domain. Ysc84 binds to actin during polymerization and requires interaction with partners like Las17/WASP for full activity, while SH3yl1 binds to liposomes, especially those with specific phosphoinositides. The document proposes two models for their function, one focusing on lipid-binding and the other on actin-binding regulated by membrane lipids, and calls for further research to clarify their mechanisms. The study was funded by the Biotechnology and Biological Sciences Research Council under grant number BB/K002511/1.
