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Traffic. 2013 Dec;14(12):1194-9. doi: 10.1111/tra.12116. Epub 2013 Sep 19.

Dynamin rings: not just for fission.

Author information

1
Nephrology Division, Massachusetts General Hospital, CNY 149 8.113, 149 13th Street, Charlestown, MA, 02129, USA.

Abstract

The GTPase dynamin has captivated researchers for over two decades, even managing to establish its own research field. Dynamin's allure is partly due to its unusual biochemical properties as well as its essential role in multiple cellular processes, which include the regulation of clathrin-mediated endocytosis and of actin cytoskeleton. On the basis of the classic model, dynamin oligomerization into higher order oligomers such as rings and helices directly executes the final fission reaction in endocytosis, which results in the generation of clathrin-coated vesicles. Dynamin's role in the regulation of actin cytoskeleton is mostly explained by its interactions with a number of actin-binding and -regulating proteins; however, the molecular mechanism of dynamin's action continues to elude us. Recent insights into the mechanism and role of dynamin oligomerization in the regulation of actin polymerization point to a novel role for dynamin oligomerization in the cell.

KEYWORDS:

dynamin actin; endocytosis; microtubules; oligomerization

PMID:
23980695
PMCID:
PMC3830594
DOI:
10.1111/tra.12116
[Indexed for MEDLINE]
Free PMC Article

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