Structural, Functional and Molecular Dynamics Examination of a de novo cloned Otopetrin-like Proton Channel in crayfish


Creative Commons License

Sağsöz M. E., Sağlam B., Arslan A. K., Baştuğ T., Çavuş M., Puralı N.

CELL BIOCHEMISTRY AND BIOPHYSICS, cilt.0, sa.0, ss.0-7, 2024 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 0 Sayı: 0
  • Basım Tarihi: 2024
  • Doi Numarası: 10.1007/s12013-024-01310-z
  • Dergi Adı: CELL BIOCHEMISTRY AND BIOPHYSICS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, BIOSIS, Biotechnology Research Abstracts, Chemical Abstracts Core, EMBASE, MEDLINE
  • Sayfa Sayıları: ss.0-7
  • Atatürk Üniversitesi Adresli: Evet

Özet

Proton channels play a crucial role in many biological functions, as they are responsible for the selective transport of protons across cell membranes. Recently, Otopetrins, a family of eukaryotic proton-selective ion channels, have attracted  significant attention due to their diverse physiological roles. Despite the importance of Otopetrins, their structural and functional properties remain relatively unexplored. As a model organism, crayfish have been extensively studied to gain insights into the functioning of the nervous system. These studies cover a wide range of aspects, including the properties of individual neurons and behavioral science. However, studying the physiological systems of crayfish poses challenges for molecular research due to limited molecular sequence information available for these organisms. In the present work was identified an originally cloned mRNA, coding an Otopetrin like proton channel in the crayfish. The coded protein was modeled in silico and possible conduction mechanisms and pathways were revealed. A plasmid of the cloned mRNA was heterologously expressed in HEK293T cells. Functional experiments on transfected cells indicated that the expressed mRNA was coupled to proton conduction across the cell membrane.
Keywords Otopetrin ● Proton channel ● Crayfish ● Molecular dynamics ● Ratio-metric fluorescence microscopy