Mineralocorticosteroid receptor

Sequence alignments of Hsp90 have shown the protein to have about 40% sequence identity across all homologs, indicating that it is a highly conserved protein. There are two homologs, found in the cytosol and endoplasmic reticulum respectively. The presence of these two homologs was likely caused by a gene duplication event very early in the evolution of eukaryotes that may have accompanied the evolution of the endoplasmic reticulum or the nucleus . This inference is supported by the fact that the duplication is found in Giardia lamblia , one of the earliest branching eukaryotic species. At least 2 other subsequent gene duplications occurred, which explains the different forms of Hsp90 found in fungi and vertebrates . One divergence produced cognate and heat-induced forms of Hsp90 in Saccharomyces cerevisiae , while the second gene duplication event in the cytosolic branch produced the alpha and beta subfamilies of sequences that are found in all vertebrates. In a phylogenetic tree based on Hsp90 sequences, it was found that plants and animals are more closely related to each other than to fungi. [66] Similar to the Hsp90 protein, the gene for Hsp70 protein also underwent duplication at a very early stage in the formation of eukaryotic cells and the homologs in the cytosol and endoplasmic reticulum resulted from this gene duplication event. [67] These gene duplication events are important in terms of the origin of the eukaryotic cell and of the endoplasmic reticulum. [68] [69]

Mineralocorticosteroid receptor

mineralocorticosteroid receptor


mineralocorticosteroid receptormineralocorticosteroid receptormineralocorticosteroid receptor