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JM4 is a four‐transmembrane protein binding to the CCR5 receptor
Author(s) -
Schweneker Marc,
Bachmann André S.,
Moelling Karin
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.02.037
Subject(s) - golgi apparatus , rab , transmembrane protein , endoplasmic reticulum , biology , microbiology and biotechnology , biochemistry , transport protein , receptor , gtpase
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.