Determining the Lipid-Binding Specificity of SMP Domains: An ERMES Subunit as a Case Study.

Andrew P AhYoung, Pascal F Egea

Open access · greenAbstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it

0cells of the map it votes in

3citing papers in PubMed

1.9field-weighted citation impact, top 13% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

Structural basis for mitoguardin-2 mediated lipid transport at ER-mitochondrial membrane contact sites.Nature communications · 2022
Article
StaR-related lipid transfer-like domain-containing protein CLDP43 affects cardiolipin synthesis and mitochondrial function in Trypanosoma brucei.PloS one · 2022
Article
Mechanisms of Non-Vesicular Exchange of Lipids at Membrane Contact Sites: Of Shuttles, Tunnels and, Funnels.Frontiers in cell and developmental biology · 2021
Review

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Andrew P AhYoungDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, CA, USA.

Pascal F EgeaDepartment of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, CA, USA. pegea@mednet.ucla.edu.

University of California, Los Angeles · US

Funding

Molecular Structure and Function of an Endoplasmic Reticulum-Mitochondrion TetherR01GM120173 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI EGEA, PASCAL FRANCOIS · 2017 to 2021

$1.5M

NIGMS NIH HHS R01 GM120173

6 · The paper itself

Abstract

Membrane contact sites between the endoplasmic reticulum (ER) and mitochondria function as a central hub for the exchange of phospholipids and calcium. The yeast Endoplasmic Reticulum-Mitochondrion Encounter Structure (ERMES) complex is composed of five subunits that tether the ER and mitochondria. Three ERMES subunits (i.e., Mdm12, Mmm1, and Mdm34) contain the synaptotagmin-like mitochondrial lipid-binding protein (SMP) domain. The SMP domain belongs to the tubular lipid-binding protein (TULIP) superfamily, which consists of ubiquitous lipid scavenging and transfer proteins. Herein, we describe the methods for expression and purification of recombinant Mdm12, a bona fide SMP-containing protein, together with the subsequent identification of its bound phospholipids by high-performance thin-layer chromatography (HPTLC) and the characterization of its lipid exchange and transfer functions using lipid displacement and liposome flotation in vitro assays with liposomes as model biological membranes. These methods can be applied to the study and characterization of novel lipid-binding and lipid-transfer proteins.

Indexed as

Protein Interaction Domains and MotifsBacteriaBiological TransportCarrier ProteinsChromatography, LiquidChromatography, Thin LayerEndoplasmic ReticulumGene Expression RegulationLiposomesMitochondrial ProteinsPhospholipidsProtein SubunitsRecombinant ProteinsStructure-Activity RelationshipYeastsCarrier Proteinslipid transfer proteinLiposomesMitochondrial ProteinsPhospholipidsProtein SubunitsRecombinant ProteinsERMESHPTLCLipid displacementLipid-transfer proteinLiposomeLiposome flotationMdm12Membrane contact sitesPhospholipidSMP domain

Identifiers

PMID30790259

DOI10.1007/978-1-4939-9136-5_16

PMCPMC6550335

OpenAlexW2917971401

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.