%0 Journal Article
%T A Tyrosine Residue on the TSH Receptor Stabilizes Multimer Formation
%A Rauf Latif
%A Krzysztof Michalek
%A Syed Ahmed Morshed
%A Terry F. Davies
%J PLOS ONE
%D 2012
%I Public Library of Science (PLoS)
%R 10.1371/journal.pone.0009449
%X The thyrotropin stimulating hormone receptor (TSHR) is a G protein coupled receptor (GPCR) with a large ectodomain. The ligand, TSH, acting via this receptor regulates thyroid growth and thyroid hormone production and secretion. The TSH receptor (TSHR) undergoes complex post ¨Ctranslational modifications including intramolecular cleavage and receptor multimerization. Since monomeric and multimeric receptors coexist in cells, understanding the functional role of just the TSHR multimers is difficult. Therefore, to help understand the physiological significance of receptor multimerization, it will be necessary to abrogate multimer formation, which requires identifying the ectodomain and endodomain interaction sites on the TSHR. Here, we have examined the contribution of the ectodomain to constitutive multimerization of the TSHR and determined the possible residue(s) that may be involved in this interaction.
%U http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0009449