Abstract
Members of the BAR domain protein superfamily are essential elements of cellular traffic. Endophilins are among the best studied BAR domain proteins. They have a prominent function in synaptic vesicle endocytosis (SVE), receptor trafficking and apoptosis, and in other processes that require remodeling of the membrane structure. Here, we discuss the role of endophilins in these processes and summarize novel insights into the molecular aspects of endophilin function. Also, we discuss phosphorylation of endophilins and how this and other mechanisms may contribute to disease.
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Note added in proof
In a recent paper (Bai et al. 2010. Cell 143: 430–441) it is demonstrated that in C. elegans endophilin null mutants, synaptic vesicle endocytosis can be rescued efficiently by endophilin protein lacking the SH3 domain, but not by protein containing a mutant N-BAR domain deficient in membrane tubulation. Another paper (Sundborger et al. J. Cell Sci., in press) provides evidence that in the lamprey synapse, endophilin recruits dynamin to a restricted part of the neck of clathrin-coated pits, forming a complex that promotes budding of new synaptic vesicles.
Acknowledgements
The authors thank Viktor Lund for critical reading of the manuscript. Supported by the Dagmar Marshall Foundation and Fonden for Lægevidenskabens Fremme (O.K, A.J.) and the Swedish Research Council/DBRM (L.B.).
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Kjaerulff, O., Brodin, L. & Jung, A. The Structure and Function of Endophilin Proteins. Cell Biochem Biophys 60, 137–154 (2011). https://doi.org/10.1007/s12013-010-9137-5
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DOI: https://doi.org/10.1007/s12013-010-9137-5