Details

Autor(en) / Beteiligte

• Kashlan, Ossama B
• Kleyman, Thomas R

Titel

ENaC structure and function in the wake of a resolved structure of a family member

Ist Teil von

• American journal of physiology. Renal physiology, 2011-10, Vol.301 (4), p.F684-F696

Ort / Verlag

United States: American Physiological Society

Erscheinungsjahr

2011

Link zum Volltext

Quelle

EZB Electronic Journals Library

Beschreibungen/Notizen

• Our understanding of epithelial Na(+) channel (ENaC) structure and function has been profoundly impacted by the resolved structure of the homologous acid-sensing ion channel 1 (ASIC1). The structure of the extracellular and pore regions provide insight into channel assembly, processing, and the ability of these channels to sense the external environment. The absence of intracellular structures precludes insight into important interactions with intracellular factors that regulate trafficking and function. The primary sequences of ASIC1 and ENaC subunits are well conserved within the regions that are within or in close proximity to the plasma membrane, but poorly conserved in peripheral domains that may functionally differentiate family members. This review examines functional data, including ion selectivity, gating, and amiloride block, in light of the resolved ASIC1 structure.