The mammalian membrane is composed of various eukaryotic lipids interacting with extensively post-translationally modified proteins. Probing interactions between these mammalian membrane proteins and their diverse and heterogeneous lipid cohort remains challenging. Recently, native mass spectrometry (MS) combined with bottom-up 'omics' approaches has provided valuable information to relate structural and functional lipids to membrane protein assemblies in eukaryotic membranes. Here we provide a step-by-step protocol to identify and provide relative quantification for endogenous lipids bound to mammalian membrane proteins and their complexes. Using native MS to guide our lipidomics strategies, we describe the necessary sample preparation steps, followed by native MS data acquisition, tailored lipidomics and data interpretation. We also highlight considerations for the integration of different levels of information from native MS and lipidomics and how to deal with the various challenges that arise during the experiments. This protocol begins with the preparation of membrane proteins from mammalian cells and tissues for native MS. The results enable not only direct assessment of copurified endogenous lipids but also determination of the apparent affinities of specific lipids. Detailed sample preparation for lipidomics analysis is also covered, along with comprehensive settings for liquid chromatography-MS analysis. This protocol is suitable for the identification and quantification of endogenous lipids, including fatty acids, sterols, glycerolipids, phospholipids and glycolipids and can be used to interrogate proteins from recombinant sources to native membranes.

Download full-text PDF

Source
http://dx.doi.org/10.1038/s41596-024-01037-4DOI Listing

Publication Analysis

Top Keywords

mammalian membrane
12
membrane proteins
12
endogenous lipids
12
quantification endogenous
8
sample preparation
8
native
7
lipids
6
lipidomics
5
membrane
5
proteins
5

Similar Publications

Transposon exonization generates new protein-coding sequences.

Mol Cell

January 2025

State Key Laboratory of Membrane Biology, Beijing Frontier Research Center for Biological Structure, Tsinghua-Peking Joint Center for Life Sciences, School of Basic Medical Sciences, Tsinghua University, Beijing 100084, China. Electronic address:

In a recent issue of Cell, Arribas et al. and Pasquesi et al. explore the phenomenon of transposable element (TE) exonization and its impact on proteomic and immune diversity, highlighting its potential role as a driver of evolutionary innovation.

View Article and Find Full Text PDF

A little protein makes big news in translation initiation.

Mol Cell

January 2025

Department of Biochemistry, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA. Electronic address:

While most of the regulation of translation initiation occurs in the cytosol predominantly through phosphorylation, Ly et al. have discovered the first instance of regulation via protein concentration due to disruption of the nuclear membrane at mitosis. Only eIF1 appears to be involved in this regulation, and its release at mitosis enhances translational accuracy of start codon recognition.

View Article and Find Full Text PDF

The cytoskeleton is a crucial determinant of mammalian cell structure and function, providing mechanical resilience, supporting the cell membrane and orchestrating essential processes such as cell division and motility. Because of its fundamental role in living cells, developing a reconstituted or artificial cytoskeleton is of major interest. Here we present an approach to construct an artificial cytoskeleton that imparts mechanical support and regulates membrane dynamics.

View Article and Find Full Text PDF

It takes two to tango: The second membrane-binding site in peripheral proteins.

Structure

January 2025

Molecular Biophysics Unit, Indian Institute of Science, Bangalore, Karnataka 560012, India. Electronic address:

In this issue of Structure, Soteriou et al. use cell biology, in vitro reconstitution approaches, and molecular dynamics (MD) simulations to characterize the membrane association of AKT1. The authors show that the AKT1 pleckstrin homology domain contains two essential and cooperative PI(3,4,5)P-binding sites that enable stable membrane binding of AKT1 in the requisite orientation required for effective downstream signaling.

View Article and Find Full Text PDF

Nowadays, food preservation, quality maintenance, and safety are major emerging concerns in the food industry. Methods for removing pathogens from the outside surfaces of food products would be an effective way to prevent bacterial contamination. Nanotopographies found on natural surfaces have been shown to mechanically damage the membranes of foodborne bacteria.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!