IMR Press / FBL / Volume 23 / Issue 10 / DOI: 10.2741/4677

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article

Homology of pendrin, sodium-iodide symporter and apical iodide transporter

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1 Department of Clinical and Experimental Medicine - Endocrinology, University of Messina, via Consolare Valeria - Gazzi, 98125 Messina, Italy
2 Master Program on Childhood, Adolescent and Women’s Endocrine Health, University of Messina, via Consolare Valeria - Gazzi, 98125 Messina, Italy
3 Interdepartmental Program on Molecular and Clinical Endocrinology and Women’s Endocrine Health, AOU Policlinico G. Martino, via Consolare Valeria - Gazzi, 98125 Messina, Italy
4 Department of Clinical and Experimental Medicine - Dermatology, University of Messina, via Consolare Valeria - Gazzi, 98125 Messina, Italy
Front. Biosci. (Landmark Ed) 2018, 23(10), 1864–1873; https://doi.org/10.2741/4677
Published: 1 June 2018
(This article belongs to the Special Issue Digging deep into thyroid pathophysiology)
Abstract

We observed local homology between human pendrin and sodium/iodide symporter (NIS), that was absent in the NIS-homologous sodium/monocarboxylate transporter or apical iodide transporter (AIT) which, however, does not transport iodide. Thus, we analyzed the full proteins. They shared 63 identical and 66 similar residues (overall homology 14.4%, but 21% when omitting intervening sequences of 15 or more residues). Pendrin was more homologous to NIS (25%) than AIT (20%), particularly in the STAS domain (sulfate transporter and antisigma factor antagonist). Homology was concentrated in 11 segments, with 3/11 involving the STAS domain. In 9/11, homology was greater with NIS (45-58.3%) than with AIT (8.3-42.3%); in 4 of these 9 segments, homology was comparable to or greater than that between NIS and AIT (8.3-52.6%). Pendrin residues which are mutated in Pendred’s syndrome are identical to those in the aligned position of NIS and AIT. Hypothyroidism-associated pendrin mutations almost always fall within 4/11 segments. These are the first data that show homology between pendrin and NIS, and topographic relationships between pendrin mutations and the hypothyroid phenotype of PDS.

Keywords
Solute carriers
pendrin
sodium/iodide symporter
apical iodide transporter
Pendred’s syndrome
iodine
amino acid sequence homology
STAS domain
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