Regulating dynamin dynamics during endocytosis
Dynamin is a large GTPase that mediates plasma membrane fission during clathrin-mediated endocytosis. Dynamin assembles into polymers on the necks of budding membranes in cells and has been shown to undergo GTP-dependent conformational changes that lead to membrane fission in vitro. Recent efforts h...
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Faculty of 1000 Ltd
2014
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4191240/ |
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pubmed-41912402014-11-05 Regulating dynamin dynamics during endocytosis Sundborger, Anna C. Hinshaw, Jenny E. Review Article Dynamin is a large GTPase that mediates plasma membrane fission during clathrin-mediated endocytosis. Dynamin assembles into polymers on the necks of budding membranes in cells and has been shown to undergo GTP-dependent conformational changes that lead to membrane fission in vitro. Recent efforts have shed new light on the mechanisms of dynamin-mediated fission, yet exactly how dynamin performs this function in vivo is still not fully understood. Dynamin interacts with a number of proteins during the endocytic process. These interactions are mediated by the C-terminal proline-rich domain (PRD) of dynamin binding to SH3 domain-containing proteins. Three of these dynamin-binding partners (intersectin, amphiphysin and endophilin) have been shown to play important roles in the clathrin-mediated endocytosis process. They promote dynamin-mediated plasma membrane fission by regulating three important sequential steps in the process: recruitment of dynamin to sites of endocytosis; assembly of dynamin into a functional fission complex at the necks of clathrin-coated pits (CCPs); and regulation of dynamin-stimulated GTPase activity, a key requirement for fission. Faculty of 1000 Ltd 2014-10-01 /pmc/articles/PMC4191240/ /pubmed/25374663 http://dx.doi.org/10.12703/P6-85 Text en © 2014 Faculty of 1000 Ltd http://creativecommons.org/licenses/by-nc/3.0/legalcode All F1000Prime Reports articles are distributed under the terms of the Creative Commons Attribution-Non Commercial License, which permits non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Sundborger, Anna C. Hinshaw, Jenny E. |
| spellingShingle |
Sundborger, Anna C. Hinshaw, Jenny E. Regulating dynamin dynamics during endocytosis |
| author_facet |
Sundborger, Anna C. Hinshaw, Jenny E. |
| author_sort |
Sundborger, Anna C. |
| title |
Regulating dynamin dynamics during endocytosis |
| title_short |
Regulating dynamin dynamics during endocytosis |
| title_full |
Regulating dynamin dynamics during endocytosis |
| title_fullStr |
Regulating dynamin dynamics during endocytosis |
| title_full_unstemmed |
Regulating dynamin dynamics during endocytosis |
| title_sort |
regulating dynamin dynamics during endocytosis |
| description |
Dynamin is a large GTPase that mediates plasma membrane fission during clathrin-mediated endocytosis. Dynamin assembles into polymers on the necks of budding membranes in cells and has been shown to undergo GTP-dependent conformational changes that lead to membrane fission in vitro. Recent efforts have shed new light on the mechanisms of dynamin-mediated fission, yet exactly how dynamin performs this function in vivo is still not fully understood. Dynamin interacts with a number of proteins during the endocytic process. These interactions are mediated by the C-terminal proline-rich domain (PRD) of dynamin binding to SH3 domain-containing proteins. Three of these dynamin-binding partners (intersectin, amphiphysin and endophilin) have been shown to play important roles in the clathrin-mediated endocytosis process. They promote dynamin-mediated plasma membrane fission by regulating three important sequential steps in the process: recruitment of dynamin to sites of endocytosis; assembly of dynamin into a functional fission complex at the necks of clathrin-coated pits (CCPs); and regulation of dynamin-stimulated GTPase activity, a key requirement for fission. |
| publisher |
Faculty of 1000 Ltd |
| publishDate |
2014 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4191240/ |
| _version_ |
1613142513433968640 |