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Biophysical Reviews

, Volume 11, Issue 3, pp 353–364 | Cite as

General and specific interactions of the phospholipid bilayer with P-type ATPases

  • Khondker R. HossainEmail author
  • Ronald J. Clarke
Review

Abstract

Protein structure and function are modulated via interactions with their environment, representing both the surrounding aqueous media and lipid membranes that have an active role in shaping the structural topology of membrane proteins. Compared to a decade ago, there is now an abundance of crystal structural data on membrane proteins, which together with their functional studies have enhanced our understanding of the salient features of lipid-protein interactions. It is now important to recognize that membrane proteins are regulated by both (1) general lipid-protein interactions, where the general physicochemical properties of the lipid environment affect the conformational flexibility of a membrane protein, and (2) by specific lipid-protein interactions, where lipid molecules directly interact via chemical interactions with specific lipid-binding sites located on the protein. However, due to local differences in membrane composition, thickness, and lipid packing, local membrane physical properties and hence the associated lipid-protein interactions also differ due to membrane location, even for the same protein. Such a phenomenon has been shown to be true for one family of integral membrane ion pumps, the P2-type adenosine triphosphatases (ATPases). Despite being highly homologous, individual members of this family have distinct structural and functional activity and are an excellent candidate to highlight how the local membrane physical properties and specific lipid-protein interactions play a vital role in facilitating the structural rearrangements of these proteins necessary for their activity. Hence in this review, we focus on both the general and specific lipid-protein interactions and will mostly discuss the structure-function relationships of the following P2-type ATPases, Na+,K+-ATPase (NKA), gastric H+,K+-ATPase (HKA), and sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA), in concurrence with their lipid environment.

Keywords

Na+,K+-ATPase Gastric H+,K+-ATPase Sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) Cholesterol Phospholipids, lipid-protein interaction 

Abbreviations

NKA

Na+,K+-ATPase

HKA

H+,K+-ATPase

SERCA

Sarco(endo)plasmic reticulum Ca2+-ATPase

TM

Transmembrane

CHL

Cholesterol

PL

Phospholipid

PC

Phosphatidylcholine

PE

Phosphatidylethanolamine

PS

Phosphatidylserine

PI

Phosphatidylinositol

SM

Sphingomyelin

Notes

Acknowledgments

The authors thank Dr. Alvaro Garcia, University of Technology Sydney, for the helpful discussions. Ronald J. Clarke acknowledges with gratitude the financial support from the Australian Research Council (Discovery Grants No. DP121003548, DP150101112, and DP170101732).

Compliance with ethical standards

Conflict of interest

Khondker R. Hossain declares that she has no conflict of interest. Ronald J. Clarke declares that he has no conflict of interest.

Ethical approval

This article does not contain any studies with human participants or animals performed by any of the authors.

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Copyright information

© International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature 2019

Authors and Affiliations

  1. 1.School of ChemistryUniversity of SydneySydneyAustralia
  2. 2.The University of Sydney Nano InstituteSydneyAustralia

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