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Vol. 16, Issue 4, 2058-2067, April 2005
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Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037
Submitted November 19, 2004;
Revised January 7, 2005;
Accepted January 29, 2005
Monitoring Editor: Suzanne Pfeffer
Dynamin, a central player in clathrin-mediated endocytosis, interacts with several functionally diverse SH3 domain-containing proteins. However, the role of these interactions with regard to dynamin function is poorly defined. We have investigated a recently identified protein partner of dynamin, SNX9, sorting nexin 9. SNX9 binds directly to both dynamin-1 and dynamin-2. Moreover by stimulating dynamin assembly, SNX9 stimulates dynamin's basal GTPase activity and potentiates assembly-stimulated GTPase activity on liposomes. In fixed cells, we observe that SNX9 partially localizes to clathrin-coated pits. Using total internal reflection fluorescence microscopy in living cells, we detect a transient burst of EGFP-SNX9 recruitment to clathrin-coated pits that occurs during the late stages of vesicle formation and coincides spatially and temporally with a burst of dynamin-mRFP fluorescence. Transferrin internalization is inhibited in HeLa cells after siRNA-mediated knockdown of SNX9. Thus, our results establish that SNX9 is required for efficient clathrin-mediated endocytosis and suggest that it functions to regulate dynamin activity.
Abbreviations used: CME, clathrin-mediated endocytosis; CCP, clathrin-coated pit; CCV, clathrin-coated vesicle; TfnR, transferrin receptor; amph1, amphyphisin-1; PI4,5P2, phosphatidyl inositol-4,5-bisphosphate; TIR-FM, total internal reflection fluorescence microscopy; WF-EF, wide-field, epifluorescence; EGFP, enhanced green fluorescent protein; mRFP, monomeric red fluorescent protein.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
Address correspondence to: Sandra L. Schmid (slschmid{at}scripps.edu).
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