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Scaffold protein assembly
Scaffold protein assembly












These condensates specifically host partners of a network relevant to cell motility, including liprin-α1, which was unnecessary for the formation of condensates, but influenced their dynamic behavior. We found that ERC1 scaffolds form cytoplasmic condensates with a behavior that is consistent with liquid phases that are modulated by a predicted disordered region of ERC1. Here by electron microscopy and single molecule analysis we identify ERC1 as an extended flexible dimer. The scaffold protein ERC1/ELKS and its partners promote cell migration and invasion, and assemble into dynamic networks at the protruding edge of cells. Scaffold proteins assemble these networks by recruiting relevant molecules. Phase separation at specific sites of the cell periphery may represent an elegant mechanism to control the assembly and turnover of dynamic scaffolds needed for the spatial localization and processing of molecules.ĪB - Several cellular processes depend on networks of proteins assembled at specific sites near the plasma membrane. N2 - Several cellular processes depend on networks of proteins assembled at specific sites near the plasma membrane. T1 - The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase Phase separation at specific sites of the cell periphery may represent an elegant mechanism to control the assembly and turnover of dynamic scaffolds needed for the spatial localization and processing of molecules.", Phase separation at specific sites of the cell periphery may represent an elegant mechanism to control the assembly and turnover of dynamic scaffolds needed for the spatial localization and processing of molecules.Ībstract = "Several cellular processes depend on networks of proteins assembled at specific sites near the plasma membrane.

scaffold protein assembly

Several cellular processes depend on networks of proteins assembled at specific sites near the plasma membrane.














Scaffold protein assembly