Syndapin – a membrane remodelling and endocytic F-BAR protein

Authors

  • Annie Quan,

    1. Cell Signalling Unit, Children's Medical Research Institute, The University of Sydney, New South Wales, Australia
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  • Phillip J. Robinson

    Corresponding author
    1. Cell Signalling Unit, Children's Medical Research Institute, The University of Sydney, New South Wales, Australia
    • Correspondence

      P. J. Robinson, Cell Signalling Unit, Children's Medical Research Institute, The University of Sydney, Locked Bag 23, Wentworthville, Sydney, New South Wales 2145, Australia

      Fax: +61 2 8865 2120

      Tel: +61 2 8865 2800

      E-mail: probinson@cmri.org.au

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Abstract

Syndapin [also called PACSIN (protein kinase C and casein kinase II interacting protein)] is an Fes-CIP4 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.

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