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J. Biol. Chem., Vol. 280, Issue 17, 17213-17220, April 29, 2005

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ATP Binding Regulates Oligomerization and Endosome Association of RME-1 Family Proteins^*

Dong-won Lee, Xiaohong Zhao, Sarah Scarselletta, Peter J. Schweinsberg¶, Evan Eisenberg, Barth D. Grant¶||, and Lois E. Greene**

From the Laboratory of Cell Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892-0301 and the ^¶Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08854

Members of the RME-1/mRme-1/EHD1 protein family have recently been shown to function in the recycling of membrane proteins from recycling endosomes to the plasma membrane. RME-1 family proteins are normally found in close association with recycling endosomes and the vesicles and tubules emanating from these endosomes, consistent with the proposal that these proteins directly participate in endosomal transport. RME-1 family proteins contain a C-terminal EH (eps15 homology) domain thought to be involved in linking RME-1 to other endocytic proteins, a coiled-coil domain thought to be involved in homo-oligomerization and an N-terminal P-loop domain thought to mediate nucleotide binding. In the present study, we show that both Caenorhabditis elegans and mouse RME-1 proteins bind and hydrolyze ATP. No significant GTP binding or hydrolysis was detected. Mutation or deletion of the ATP-binding P-loop prevented RME-1 oligomerization and at the same time dissociated RME-1 from endosomes. In addition, ATP depletion caused RME-1 to lose its endosome association in the cell, resulting in cytosolic localization. Taken together, these results indicate that ATP binding is required for oligomerization of mRme-1/EHD1, which in turn is required for its association with endosomes.

Received for publication, November 10, 2004 , and in revised form, February 11, 2005.

^* This work was supported in part by National Institutes of Health Grant GM67237-01 (to B. D. G.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains a supplemental figure showing the requirements for Ce-RME-1 oligomerization.

Both authors contributed equally to this work.

^|| A recipient of support from the Chicago Community Trust Searle Scholars Program.

^** To whom correspondence should be addressed: Laboratory of Cell Biology, NHLBI, National Institutes of Health, 50 South Dr., Rm. 2537 MSC 8017, Bethesda, MD 20892-8017. Tel.: 301-496-1228; E-mail: greenel{at}helix.nih.gov.

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