Identification of the invariant chain (CD74) as an angiotensin AGTR1-interacting protein

The Journal of Endocrinology
Márta SzaszákKevin J Catt

Abstract

Little is known about the protein-protein interactions that regulate the trafficking of the angiotensin II type I receptor (AGTR1) through the biosynthetic pathway. The membrane-proximal region of the cytoplasmic tail of the AGTR1 has been identified by site-directed mutagenesis studies as an essential site for normal AGTR1 folding and surface expression. Based on yeast two-hybrid screening of a human kidney cDNA library with the AGTR1 carboxyl-terminal tail as a bait, we identified the invariant chain (CD74) as a novel interacting protein. This association was confirmed by co-immunoprecipitation and co-localization studies. The binding site for CD74 on the AGTR1 carboxyl-terminal tail was localized to a site previously identified as important for the exit of the AGTR1 from the endoplasmic reticulum (ER), and conserved in many G protein-coupled receptors. Transient co-expression of CD74 with the AGTR1 in CHO-K1 cells consistently reduced the AGTR1 density at the cell surface. Furthermore, the interaction of CD74 with the carboxyl-terminal tail of the AGTR1 caused its retention in the ER and promoted its proteasomal degradation. These observations indicate that CD74 and the AGTR1 become associated in the early biosynthetic pathw...Continue Reading

Citations

Jan 23, 2010·Journal of the American Society of Nephrology : JASN·Mona OppermannHayo Castrop
Aug 12, 2009·FEBS Letters·Verena SchwartzJürgen Bernhagen
Sep 11, 2012·Cytokine & Growth Factor Reviews·M D Sanchez-NiñoA Ortiz
Sep 1, 2015·Cellular Immunology·Denise A Le NouryRaymond Hewer
Apr 2, 2016·Biochimica Et Biophysica Acta·Bernd Schröder
Oct 7, 2015·Frontiers in Immunology·Lara Valiño-RivasMaria Dolores Sanchez-Niño
Oct 19, 2016·Inflammation Research : Official Journal of the European Histamine Research Society ... [et Al.]·Huiting SuYong Zhao
Feb 24, 2012·American Journal of Physiology. Renal Physiology·Elisabeth DoblingerHayo Castrop

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