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J. Biol. Chem., Vol. 278, Issue 38, 36032-36040, September 19, 2003
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-ALZHEIMER'S PRECURSOR PROTEIN*
From the
Department of Biochemistry, the ¶Department of Neurology, and ||Center for Neurodegenerative Diseases, School of Medicine, Emory University, Atlanta, Georgia 30322-3050 and IGEN International Corporation, Gaithersburg, Maryland 20877
Coat proteins cycle between soluble and membrane-bound locations at the time of vesicle biogenesis and act to regulate the assembly of the vesicle coat that determines the specificity in cargo selection and the destination of the vesicle. A transmembrane cargo protein, an Arf GTPase, and a coat protein (e.g. COPs, APs, or GGAs) are minimal components required for budding of vesicles. Munc18 interacting proteins (MINTs) are a family of three proteins implicated in the localization of receptors to the plasma membrane. We show that MINTs bind Arfs directly, co-localize with Arf and the Alzheimer's precursor protein (-APP) to regions of the Golgi/trans-Golgi network, and can co-immunoprecipitate clathrin. We demonstrate that MINTs bind Arfs through a region of the PTB domain and the PDZ2 domain, and Arf-MINT interaction is necessary for the increased cellular levels of -APP produced by MINT overexpression. Knockdown (small interference RNA) experiments implicate -APP as a transmembrane cargo protein that works together with MINTs. We propose that MINTs are a family of Arf-dependent, vesicle-coat proteins that can regulate the traffic of -APP.
Received for publication, February 14, 2003 , and in revised form, June 25, 2003.
* 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.
** To whom correspondence should be addressed: Center for Neurodegenerative Diseases, Emory University School of Medicine, 1510 Clifton Rd., Atlanta, GA 30322-3050. Tel.: 404-727-3561; Fax: 404-727-3746; E-mail: rkahn{at}emory.edu.
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