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A more recent version of this article appeared on September 19, 2003
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M301632200v1
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Papers In Press, published online ahead of print July 3, 2003
J. Biol. Chem, 10.1074/jbc.M301632200
Submitted on February 14, 2003
Revised on June 25, 2003
Accepted on July 3, 2003

Munc 18 Interacting (MINT) Proteins: Arf-dependent coat proteins that regulate traffic of the Alzheimer's precursor protein (beta-APP)

Karen Hill, Yawei Li, Matthew Bennett, Melissa McKay, Xinjun Zhu, Jack Shern, Enrique Torre, James J. Lah, Allan I. Levey, and Richard A. Kahn

Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322-3050

Corresponding Author: rkahn{at}emory.edu

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. 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 (b- APP) to regions of the Golgi/TGN, 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 ß-APP produced by MINT over-expression. Knockdown (siRNA) experiments implicate b-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 b-APP.


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