Journal
FEBS JOURNAL
Volume 280, Issue 21, Pages 5198-5212Publisher
WILEY
DOI: 10.1111/febs.12343
Keywords
actin cytoskeleton; autoinhibition; bulk endocytosis; dynamin; N-WASP; PACSIN; phosphorylation; syndapin
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Funding
- Australian National Health and Medical Research Council
- Ramaciotti Foundation
- Cancer Institute NSW
- Australian Cancer Research Foundation
- Ian Potter Foundation
- CMRI Postgraduate Research Scholarship
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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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