본문 바로가기
HOME> 논문 > 논문 검색상세

논문 상세정보

Biophysical journal v.112 no.2, 2017년, pp.288 - 299   SCI SCIE
본 등재정보는 저널의 등재정보를 참고하여 보여주는 베타서비스로 정확한 논문의 등재여부는 등재기관에 확인하시기 바랍니다.

Electrostatic Stabilization Plays a Central Role in Autoinhibitory Regulation of the Na+,K+-ATPase

Jiang, Qiucen (Nanjing University, Jiangsu Sheng, China ); Garcia, Alvaro (School of Chemistry, The University of Sydney, Sydney, New South Wales, Australia ); Han, Minwoo (MEMPHYS, Center for Biomembrane Physics, University of Southern Denmark, Odense, Denmark ); Cornelius, Flemming (Department of Biomedicine, University of Aarhus, Aarhus, Denmark ); Apell, Hans-Jürgen (Faculty of Biology, University of Konstanz, Konstanz, Germany ); Khandelia, Himanshu (MEMPHYS, Center for Biomembrane Physics, University of Southern Denmark, Odense, Denmark ); Clarke, Ronald J. (School of Chemistry, The University of Sydney, Sydney, New South Wales, Australia );
  • 초록  

    Abstract The Na + ,K + -ATPase is present in the plasma membrane of all animal cells. It plays a crucial role in maintaining the Na + and K + electrochemical potential gradients across the membrane, which are essential in numerous physiological processes, e.g., nerve, muscle, and kidney function. Its cellular activity must, therefore, be under tight metabolic control. Consideration of eosin fluorescence and stopped-flow kinetic data indicates that the enzyme’s E2 conformation is stabilized by electrostatic interactions, most likely between the N-terminus of the protein’s catalytic α -subunit and the adjacent membrane. The electrostatic interactions can be screened by increasing ionic strength, leading to a more evenly balanced equilibrium between the E1 and E2 conformations. This represents an ideal situation for effective regulation of the Na + ,K + -ATPase’s enzymatic activity, because protein modifications, which perturb this equilibrium in either direction, can then easily lead to activation or inhibition. The effect of ionic strength on the E1:E2 distribution and the enzyme’s kinetics can be mathematically described by the Gouy-Chapman theory of the electrical double layer. Weakening of the electrostatic interactions and a shift toward E1 causes a significant increase in the rate of phosphorylation of the enzyme by ATP. Electrostatic stabilization of the Na + ,K + -ATPase’s E2 conformation, thus, could play an important role in regulating the enzyme’s physiological catalytic turnover.


 활용도 분석

  • 상세보기

    amChart 영역
  • 원문보기

    amChart 영역

원문보기

무료다운로드
  • 원문이 없습니다.

유료 다운로드의 경우 해당 사이트의 정책에 따라 신규 회원가입, 로그인, 유료 구매 등이 필요할 수 있습니다. 해당 사이트에서 발생하는 귀하의 모든 정보활동은 NDSL의 서비스 정책과 무관합니다.

원문복사신청을 하시면, 일부 해외 인쇄학술지의 경우 외국학술지지원센터(FRIC)에서
무료 원문복사 서비스를 제공합니다.

NDSL에서는 해당 원문을 복사서비스하고 있습니다. 위의 원문복사신청 또는 장바구니 담기를 통하여 원문복사서비스 이용이 가능합니다.

이 논문과 함께 출판된 논문 + 더보기