Mapping pathogenic mutations suggests an innovative structural model for the pendrin (SLC26A4) transmembrane domain

Biochimie. 2017 Jan:132:109-120. doi: 10.1016/j.biochi.2016.10.002. Epub 2016 Oct 19.

Abstract

Human pendrin (SLC26A4) is an anion transporter mostly expressed in the inner ear, thyroid and kidney. SLC26A4 gene mutations are associated with a broad phenotypic spectrum, including Pendred Syndrome and non-syndromic hearing loss with enlarged vestibular aqueduct (ns-EVA). No experimental structure of pendrin is currently available, making phenotype-genotype correlations difficult as predictions of transmembrane (TM) segments vary in number. Here, we propose a novel three-dimensional (3D) pendrin transmembrane domain model based on the SLC26Dg transporter. The resulting 14 TM topology was found to include two non-canonical transmembrane segments crucial for pendrin activity. Mutation mapping of 147 clinically validated pathological mutations shows that most affect two previously undescribed TM regions.

Keywords: Homology modeling; Mutation mapping; Non-syndromic hearing loss with enlarged vestibular aqueduct (ns-EVA); Pendred syndrome; Pendrin; SLC26A4; Transmembrane protein.

MeSH terms

  • Amino Acid Motifs / genetics
  • Amino Acid Sequence
  • Genetic Predisposition to Disease / genetics*
  • Goiter, Nodular / genetics
  • Hearing Loss, Sensorineural / genetics
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics*
  • Membrane Transport Proteins / chemistry
  • Membrane Transport Proteins / genetics*
  • Models, Molecular
  • Mutation*
  • Protein Domains
  • Protein Structure, Secondary
  • Sequence Homology, Amino Acid
  • Sulfate Transporters
  • Vestibular Aqueduct / abnormalities

Substances

  • Membrane Proteins
  • Membrane Transport Proteins
  • SLC26A4 protein, human
  • Sulfate Transporters

Supplementary concepts

  • Deafness, Autosomal Recessive 4
  • Pendred syndrome