REVIEW Plant lipid environment and membrane enzymes: the case of the plasma membrane H + -ATPase Francisco Morales-Cedillo • Ariadna Gonza ´lez-Solı ´s • Lizbeth Gutie ´rrez-Angoa • Dora Luz Cano-Ramı ´rez • Marina Gavilanes-Ruiz Received: 1 October 2014 / Revised: 18 December 2014 / Accepted: 29 December 2014 Ó Springer-Verlag Berlin Heidelberg 2015 Abstract Several lipid classes constitute the universal matrix of the biological membranes. With their amphi- pathic nature, lipids not only build the continuous barrier that confers identity to every cell and organelle, but they are also active actors that modulate the activity of the proteins immersed in the lipid bilayer. The plasma mem- brane H ? -ATPase, an enzyme from plant cells, is an excellent example of a transmembrane protein whose activity is influenced by the hydrophilic compartments at both sides of the membrane and by the hydrophobic domains of the lipid bilayer. As a result, an extensive documentation of the effect of numerous amphiphiles in the enzyme activity can be found. Detergents, membrane glycerolipids, and sterols can produce activation or inhi- bition of the enzyme activity. In some cases, these effects are associated with the lipids of the membrane bulk, but in others, a direct interaction of the lipid with the protein is involved. This review gives an account of reports related to the action of the membrane lipids on the H ? -ATPase activity. Keywords H ? -ATPase Á Membrane lipids Á Plant plasma membrane Á Protein–lipid interaction Abbreviations ABA Abscisic acid A. thaliana Arabidopsis thaliana ATP Adenosine triphosphate A. sativa Avena sativa CMC Critical micelle concentration FA Fatty acid FB 1 Fumonisin B 1 GA3 Gibberellic acid 3 LCB Long-chain base LPC Lysophosphatidylcholine N. tabacum Nicotiana tabacum PA Phosphatidic acid PC Phosphatidylcholine PE Phosphatidylethanolamine PG Phosphatidylglycerol PI Phosphatidylinositol PM H ? -ATPase Plasma membrane H ? -ATPase Pma1 Yeast plasma membrane H ? -ATPase, isoform 1 PS Phosphatidylserine V. radiata Vigna radiata The amphipathicity of the membrane lipids in aqueous environments: a challenge for studying the topology of the membrane proteins Analysis of the structure of hydrophilic proteins by X-ray crystallography has revealed the importance of the milieu in which proteins are embedded. The polypeptide chains of membrane proteins, especially those that are transmem- brane, are subjected to media of varying polarity, molec- ular mobility, and order degree as the chain traverses the lipid bilayer. Thus, outside of the bilayer, the protein hydrophilic domains are exposed to the dipolar water Communicated by Neal Stewart. F. Morales-Cedillo Á A. Gonza ´lez-Solı ´s Á L. Gutie ´rrez-Angoa Á D. L. Cano-Ramı ´rez Á M. Gavilanes-Ruiz (&) Dpto. de Bioquı ´mica, Facultad de Quı ´mica, Conj. E. Universidad Nacional Auto ´noma de Me ´xico, UNAM. Cd. Universitaria, Coyoaca ´n, 04510 Mexico, D.F., Mexico e-mail: gavilan@unam.mx 123 Plant Cell Rep DOI 10.1007/s00299-014-1735-z