Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10872904 | FEBS Letters | 2005 | 8 Pages |
Abstract
The CC chemokine receptor 5 (CCR5) is a major co-receptor for human immunodeficiency virus (HIV) and CCR5 mutants lacking the carboxy (C)-terminus interfere with HIV infection. Therefore, we analysed the C-terminus of CCR5 and here describe Jena-Muenchen 4 (JM4), a novel CCR5-interacting protein. JM4 is membrane-associated, co-precipitates with CCR5, and is ubiquitously expressed. It shares about 62% sequence similarity with JWA and glutamate transporter-associated protein 3-18 (GTRAP3-18), a regulator of an amino acid transporter. JWA, like JM4, is a four-transmembrane protein, which binds to the CCR5 receptor. Furthermore, JM4, JWA, and GTRAP3-18 co-localise and heterodimerise indicating a functional relationship. JM4 co-localises with calnexin in the endoplasmic reticulum and with the mannose 6-phosphate receptor in the Golgi. JM4 and GTRAP3-18 harbor a Rab-acceptor motif, indicating a function in vesicle formation at the Golgi complex. In conclusion, we describe a CCR5-interacting protein, which is suggested to function in trafficking and membrane localisation of the receptor, possibly also other receptors or amino acid transporters.
Keywords
CC chemokine receptor 5M6PRCarboxyPra1TGNVSVARFARLCCR5GPCREAAC1CDDAminoexcitatory amino acid carrier 1Trans-Golgi networkendoplasmic reticulumADP-ribosylation factorIntracellular traffickinghemagglutininVesicular stomatitis virusHIV-1Human immunodeficiency virus type 1conserved domain databaseGolgiMannose 6-phosphate receptorG protein-coupled receptor
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Authors
Marc Schweneker, André S. Bachmann, Karin Moelling,