Journal
ELIFE
Volume 6, Issue -, Pages -Publisher
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.26856
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Funding
- H European Research Council [311536]
- Schweizerischer Nationalfonds zur Forderung der Wissenschaftlichen Forschung [31003A_130520, 31003A_149975]
- Human Frontier Science Program [CDA-0061-08]
- National Institutes of Health [1DP2GM110772, N5036251]
- Howard Hughes Medical Institute [55108523]
- Searle scholars award [13SSP218]
- TRANSPOL [264399]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [DP2GM110772, R01GM127673] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R37NS036251, R01NS036251] Funding Source: NIH RePORTER
- OFFICE OF THE DIRECTOR, NATIONAL INSTITUTES OF HEALTH [S10OD020054, S10OD021741, S10OD021596] Funding Source: NIH RePORTER
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Dynamin, which mediates membrane fission during endocytosis, binds endophilin and other members of the Bin-Amphiphysin-Rvs (BAR) protein family. How endophilin influences endocytic membrane fission is still unclear. Here, we show that dynamin-mediated membrane fission is potently inhibited in vitro when an excess of endophilin co-assembles with dynamin around membrane tubules. We further show by electron microscopy that endophilin intercalates between turns of the dynamin helix and impairs fission by preventing trans interactions between dynamin rungs that are thought to play critical roles in membrane constriction. In living cells, overexpression of endophilin delayed both fission and transferrin uptake. Together, our observations suggest that while endophilin helps shape endocytic tubules and recruit dynamin to endocytic sites, it can also block membrane fission when present in excess by inhibiting inter-dynamin interactions. The sequence of recruitment and the relative stoichiometry of the two proteins may be critical to regulated endocytic fission.
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