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Syndapin – a membrane remodelling and endocytic F‐ BAR protein
Author(s) -
Quan Annie,
Robinson Phillip J.
Publication year - 2013
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12343
Subject(s) - amphiphysin , endocytic cycle , microbiology and biotechnology , endocytosis , proto oncogene tyrosine protein kinase src , biology , sh3 domain , signal transducing adaptor protein , cytoskeleton , phosphorylation , chemistry , dynamin , biochemistry , receptor , cell
Syndapin [also called PACSIN (protein kinase C and casein kinase II interacting protein)] is an Fes‐ CIP 4 homology Bin‐amphiphysin‐Rvs161/167 (F‐ BAR ) and Src‐homology 3 domain‐containing protein. Three genes give rise to three main isoforms in mammalian cells. 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. 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. Its various partner proteins provide insights into its mechanism of action, as well as its differential roles in these cellular processes. 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.