TY - JOUR
T1 - Solubilization of human cells by the styrene-maleic acid copolymer
T2 - Insights from fluorescence microscopy
AU - Dörr, Jonas M
AU - van Coevorden-Hameete, Marleen H
AU - Hoogenraad, Casper C
AU - Killian, J Antoinette
N1 - Copyright © 2017 Elsevier B.V. All rights reserved.
PY - 2017/11
Y1 - 2017/11
N2 - Extracting membrane proteins from biological membranes by styrene-maleic acid copolymers (SMAs) in the form of nanodiscs has developed into a powerful tool in membrane research. However, the mode of action of membrane (protein) solubilization in a cellular context is still poorly understood and potential specificity for cellular compartments has not been investigated. Here, we use fluorescence microscopy to visualize the process of SMA solubilization of human cells, exemplified by the immortalized human HeLa cell line. Using fluorescent protein fusion constructs that mark distinct subcellular compartments, we found that SMA solubilizes membranes in a concentration-dependent multi-stage process. While all major intracellular compartments were affected without a strong preference, plasma membrane solubilization was found to be generally slower than the solubilization of organelle membranes. Interestingly, some plasma membrane-localized proteins were more resistant against solubilization than others, which might be explained by their presence in specific membrane domains with differing properties. Our results support the general applicability of SMA for the isolation of membrane proteins from different types of (sub)cellular membranes.
AB - Extracting membrane proteins from biological membranes by styrene-maleic acid copolymers (SMAs) in the form of nanodiscs has developed into a powerful tool in membrane research. However, the mode of action of membrane (protein) solubilization in a cellular context is still poorly understood and potential specificity for cellular compartments has not been investigated. Here, we use fluorescence microscopy to visualize the process of SMA solubilization of human cells, exemplified by the immortalized human HeLa cell line. Using fluorescent protein fusion constructs that mark distinct subcellular compartments, we found that SMA solubilizes membranes in a concentration-dependent multi-stage process. While all major intracellular compartments were affected without a strong preference, plasma membrane solubilization was found to be generally slower than the solubilization of organelle membranes. Interestingly, some plasma membrane-localized proteins were more resistant against solubilization than others, which might be explained by their presence in specific membrane domains with differing properties. Our results support the general applicability of SMA for the isolation of membrane proteins from different types of (sub)cellular membranes.
KW - Journal Article
KW - Native nanodiscs
KW - SMA-resistant membranes
KW - Preferential solubilization
KW - Cellular localization
KW - Plasma membrane organization
KW - Membrane domain
U2 - 10.1016/j.bbamem.2017.08.010
DO - 10.1016/j.bbamem.2017.08.010
M3 - Article
C2 - 28847501
SN - 0006-3002
VL - 1859
SP - 2155
EP - 2160
JO - Biochimica et Biophysica Acta
JF - Biochimica et Biophysica Acta
IS - 11
ER -