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. 2019 Dec 10;122(2):266–278. doi: 10.1038/s41416-019-0675-3

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — Mia PaCa-2 cells were incubated with sulfo-NHS-SS-Biotin, which binds to primary amines on cell surface/transmembrane proteins. These biotinylated proteins were separated from non-biotinylated proteins using NeutrAvidin^TM agarose beads and eluted using dithiothreitol. Whole-cell lysates (Lys), non-biotinylated (NB) and biotinylated (Biot) fractions were separated by SDS-PAGE and western blotted for the membrane proteins, PMCA4 (ai) and non-specific (NS) PMCA (aii), the glycolytic enzymes, phosphofructokinase-1 (PFK1, bi), phosphofructokinase fructose bisphosphatase-3 (PFKFB3, bii) and pyruvate kinase-M2 (PKM2, biii), lactate dehydrogenase (LDH, biv), glyceraldehyde phosphate dehydrogenase (GAPDH, bv), hexokinase-I (HKI, bvi) and the mitochondria-associated proteins hexokinase-II (HKII, ci) and pyruvate dehydrogenase (PDH, cii). d Cartoon depicting a complex of key glycolytic enzymes associated with the plasma membrane (membrane glycolytic metabolon) in close proximity to glucose transporters (GLUT), lactate transporters (MCT) and the PMCA.