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J. Biol. Chem., Vol. 277, Issue 24, 21650-21656, June 14, 2002
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From the Department of Physiology, Semmelweis University,
Faculty of Medicine, H-1088 Budapest, Hungary, the
In nonneural tissues, the
dynamin-2 isoform participates in the formation of clathrin-coated
vesicles during receptor endocytosis. In this study, the mechanism of
dynamin-2 action was explored during endocytosis of the G
protein-coupled AT1A angiotensin receptor expressed
in Chinese hamster ovary cells. Dynamin-2 molecules with mutant
pleckstrin homology domains or deleted proline-rich domains (PRD)
exerted dominant negative inhibition on the endocytosis of radiolabeled
angiotensin II. However, only the PRD mutation interfered with the
localization of the dynamin-2 molecule to clathrin-coated pits and
reduced the inhibitory effect of the GTPase-deficient K44A mutant
dynamin-2. Green fluorescent protein-tagged Src homology 3 (SH3)
domains of endophilin I and amphiphysin II, two major binding partners
of dynamins, also inhibited AT1A receptor-mediated endocytosis of angiotensin II. These effects were partially or fully,
respectively, restored by the overexpression of dynamin-2. Transient
overexpression of these SH3 domains also reduced the localization of
dynamin-2 to clathrin-coated pits. These data indicate that, similar to
the recruitment of dynamin-1 during the recycling of synaptic vesicles,
interaction of the dynamin-2 PRD with SH3 domains of proteins such as
the amphiphysins and endophilins is essential for AT1A
receptor endocytosis. This mechanism could be of general importance in
dynamin-dependent endocytosis of other G protein-coupled
receptors in nonneural tissues.
Role of the Proline-rich Domain of Dynamin-2
and Its Interactions with Src Homology 3 Domains during Endocytosis of
the AT1 Angiotensin Receptor*
,
Department of Neurology and Neurosurgery, Montreal
Neurological Institute, McGill University, Montreal, Quebec H3A
2B4, Canada, the § Department of Endocrinology, Barts & the
London, Queen Mary, University of London, London EC1A 7BE, United
Kingdom, and ¶ Endocrinology and Reproduction Research Branch,
NICHD, National Institutes of Health,
Bethesda, Maryland 20892-4510
*
This work was supported in part by Wellcome Trust
Collaborative Research Initiative Grant 051804/Z/97/Z, Hungarian
Ministry of Education Grants FKFP-0318/1999 and OMFB 02489/2000,
Hungarian Science Foundation Grant OTKA T-032179, Hungarian Ministry of Health Grant ETT 315/2000, and Canadian Institutes of Health Research Operating Grant MT-1346 (endophilin grant).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Physiology, Semmelweis University, Faculty of Medicine, H-1444
Budapest, 8. P.O. Box 259, Hungary. Tel.: 36-1-266-2755 (ext. 4041);
Fax: 36-1-266-6504; E-mail: Hunyady@puskin.sote.hu.
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