Evidence map›Paper›PMID 36056103›Full record

ReviewNature reviews. Molecular cell biology2023

Regulation of membrane protein structure and function by their lipid nano-environment.

Ilya Levental, Ed Lyman

Erratum issuedOpen access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 319 papers.

0numbers the graph read from it
0cells of the map it votes in
319citing papers in PubMed
41.3field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

319 citing papers in PubMed, 522 citations in OpenAlex.

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  16. Molecular mechanisms of Kir channel gating.Biochemical Society transactions · 2026
    Review
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259 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Ilya LeventalDepartment of Molecular Physiology and Biological Physics, Center for Molecular and Cell Physiology, University of Virginia, Charlottesville, VA, USA. il2sy@virginia.edu.ORCID 0000-0002-1206-9545
Ed LymanDepartment of Physics and Astronomy, Department of Chemistry and Biochemistry, University of Delaware, Newark, DE, USA. elyman@udel.edu.ORCID 0000-0003-4590-0363
University of Delaware · USUniversity of Virginia · US

Funding

The functional organization of mammalian membranes-Equipment SupplementR35GM134949 · NIGMS · UNIVERSITY OF VIRGINIA · PI Ilya Levental · 2020 to 2026
$3.8M
Effects of lipidomic diversity on GPCRR01GM120351 · NIGMS · UNIVERSITY OF DELAWARE · PI LYMAN, EDWARD RAY · 2017 to 2021
$1.6M
Structural determinants and functional consequences of protein partitioning to ordered membrane microdomains.R01GM124072 · NIGMS · UNIVERSITY OF VIRGINIA · PI LEVENTAL, ILYA · 2017 to 2019
$961k
NIGMS NIH HHS R01 GM120351NIGMS NIH HHS R01 GM124072NIGMS NIH HHS R35 GM134949
6 · The paper itself

Abstract

Transmembrane proteins comprise ~30% of the mammalian proteome, mediating metabolism, signalling, transport and many other functions required for cellular life. The microenvironment of integral membrane proteins (IMPs) is intrinsically different from that of cytoplasmic proteins, with IMPs solvated by a compositionally and biophysically complex lipid matrix. These solvating lipids affect protein structure and function in a variety of ways, from stereospecific, high-affinity protein-lipid interactions to modulation by bulk membrane properties. Specific examples of functional modulation of IMPs by their solvating membranes have been reported for various transporters, channels and signal receptors; however, generalizable mechanistic principles governing IMP regulation by lipid environments are neither widely appreciated nor completely understood. Here, we review recent insights into the inter-relationships between complex lipidomes of mammalian membranes, the membrane physicochemical properties resulting from such lipid collectives, and the regulation of IMPs by either or both. The recent proliferation of high-resolution methods to study such lipid-protein interactions has led to generalizable insights, which we synthesize into a general framework termed the 'functional paralipidome' to understand the mutual regulation between membrane proteins and their surrounding lipid microenvironments.

Indexed as

Membrane ProteinsProteomeAnimalsCell MembraneLipidsMammalsLipidsMembrane ProteinsProteome

Identifiers

PMID36056103
PMCPMC9892264
OpenAlexW4294275581

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.