The latter residues interact with negatively-charged phospholipid membranes. Each shares common BAR domain defining elements: elongated homodimers of six α-helical coiled coils, characterized by a curvature that positions a set of positive residues on one surface. There are several subfamilies based on structural analyses and sequence homologies: the classical BAR, the N-terminal amphipathic α-helix BAR, the BAR-pleckstrin homology, the PhoX-BAR, the Fes-CIP4 homology BAR (F-BAR) and the inverse-BAR domain. BAR domains act as scaffolds to form a high-curvature membrane structure. BAR domains are found in a large number of diverse proteins that confers on that protein the ability to detect membrane curvature and further shape the membrane. One lipid binding and remodelling domain commonly found in proteins is the Bin-amphiphysin-Rvs161/167 (BAR) family. These processes are mainly achieved by two classes of modular protein domains that mediate protein–protein interactions or that bind and remodel cell membranes. Rapid responses can be achieved by signal transduction pathways, leading to the recruitment of proteins to assist in shaping and remodelling the membrane at the right place and time. This depends on the components that are present and how they are spatially distributed. The ability of a membrane to achieve this is determined by the local shape and composition of lipids and proteins in the membrane at the site where such processes will occur. Many cellular processes require dynamic changes at the plasma membrane to form vesicles, endosomes, large vacuoles, tubules or filopodia within seconds to minutes. 90-kDa Nck-interacting protein with a SH3 domain.neural Wiskott–Aldrich syndrome protein.Fes-CIP4 homology Bin-amphiphysin-Rvs161/167.Signalling pathways leading to the regulation of syndapin function by phosphorylation are now contributing to our understanding of the broader functions of this family of proteins. Its various partner proteins provide insights into its mechanism of action, as well as its differential roles in these cellular processes. The membrane remodelling activity of syndapin via its F-BAR domain and its interaction partners, such as dynamin and neural Wiskott–Aldrich syndrome protein binding to its Src-homology 3 domain, are important with respect to its function.
They each function in different endocytic and vesicle trafficking pathways and provide critical links between the cytoskeletal network in different cellular processes, such as neuronal morphogenesis and cell migration. Three genes give rise to three main isoforms in mammalian cells. Syndapin is an Fes-CIP4 homology Bin-amphiphysin-Rvs161/167 (F-BAR) and Src-homology 3 domain-containing protein.
0 kommentar(er)
