Dataset Information

Composition of raft-like cell membrane microdomains resistant to styrene-maleic acid copolymer (SMA) solubilization

ABSTRACT: An advantageous alternative to the use of detergents in biochemical studies on membrane proteins have recently been styrene-maleic acid (SMA) amphipathic copolymers. These cut the membrane into nanodiscs (often called SMA-lipid particles, SMALPs), which contain membrane proteins surrounded by their relatively native lipid environment. In our recent study [1] we demonstrated that using this approach, most T cell membrane proteins were fully solubilized (presumably in small nanodiscs), while two types of raft proteins, GPI-anchored proteins and Src family kinases, were mostly present in much larger (>250 nm) membrane fragments markedly enriched in typical raft lipids, cholesterol and lipids containing saturated fatty acid residues. In the present study we demonstrate that disintegration of membranes of several other cell types by means of SMA copolymer follows a similar pattern and we provide a detailed proteomic and lipidomic characterization of these SMA-resistant membrane fragments (SRMs).

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Karel Harant

LAB HEAD: Václav Hořejší

PROVIDER: PXD031828 | Pride | 2023-07-26

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	1026-horejsi_test_20211217135609.CID.ITMS.peak.apl	Other
	1026-horejsi_test_20211217135609.HCD.ITMS.peak.apl	Other
	1026-horejsi_test_20211217135609.raw	Raw
	20210127_human_rew_uni.fasta	Fasta
	20210712_human_uni_trembl.fasta	Fasta

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Composition of raft-like cell membrane microdomains resistant to styrene-maleic acid copolymer (SMA) solubilization.

Harant Karel K Čajka Tomáš T Angelisová Pavla P Pokorná Jana J Hořejší Václav V

Biophysical chemistry 20230305

An advantageous alternative to the use of detergents in biochemical studies on membrane proteins are the recently developed styrene-maleic acid (SMA) amphipathic copolymers. In our recent study <sup>[1]</sup> we demonstrated that using this approach, most T cell membrane proteins were fully solubilized (presumably in small nanodiscs), while two types of raft proteins, GPI-anchored proteins and Src family kinases, were mostly present in much larger (>250 nm) membrane fragments markedly enriched i ...[more]

PMID: 36898346

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