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    Home > Biochemistry News > Biotechnology News > Structural basis for autoinhibition of the human NHE3-CHP1 complex

    Structural basis for autoinhibition of the human NHE3-CHP1 complex

    • Last Update: 2022-08-11
    • Source: Internet
    • Author: User
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    Summary

    Sodium proton exchanger 3 (NHE3/SLC9A3) is located on the apical membrane of the renal and gastrointestinal epithelium, mediates salt and fluid absorption, and regulates pH homeostas.


    Calcineurin B homologous protein 1 (CHP1) acts as a co-regulator of NHE proteins, promoting NHE3 maturation, plasma membrane expression, and pH sensitivi.


    Introduction

    Not applicable

    +/H+Exchange or anti-transporters (NHEs/NHAs) are integral membrane secondary active transporters present in all organisms examined to date, a notion that supports their origin in an early stage of biosphere evolution (1


    In recent years, mammalian NHE1 and NHE9 structures have been reported (11,12


    For example, NHE1 and NHE3 are known to bind to calcineurin B homolog protein 1 (CHP1), which contributes to maturation, cell surface expression and transporter function (18


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