Evidence map›Paper›PMID 38464273›Full record

ArticlebioRxiv : the preprint server for biology2025

PILS-Nir1 is a novel phosphatidic acid biosensor that reveals mechanisms of lipid production.

Claire C Weckerly, Taylor A Rahn, Max Ehrlich, Rachel C Wills, Joshua G Pemberton, Michael V Airola, Gerald R V Hammond

Open access · greenAbstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Claire C WeckerlyDepartment of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.ORCID 0000-0003-2368-8429
Taylor A RahnDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY, USA.ORCID 0000-0002-5031-6914
Max EhrlichDepartment of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.ORCID 0000-0003-3975-5788
Rachel C WillsDepartment of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.ORCID 0000-0003-2161-9235
Joshua G PembertonSection on Molecular Signal Transduction, Program for Developmental Neuroscience, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, MD, USA.ORCID 0000-0002-1492-1471
Michael V AirolaDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY, USA.ORCID 0000-0003-4981-1253
Gerald R V HammondDepartment of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.ORCID 0000-0002-6660-3272
University of Pittsburgh · USStony Brook University · USNational Institutes of Health · US

Funding

Directing Membrane Function with Inositol Lipids in Health and DiseaseR35GM119412 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Gerald R Hammond · 2016 to 2026
$4.3M
Structure and regulation of lipid metabolism and transportR35GM128666 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI Michael Virgil Airola · 2018 to 2026
$4.0M
The roles of PLD and DGK isoforms in PIP2 homeostasis during PLC signalingF31HL170755 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI WECKERLY, CLAIRE · 2023 to 2025
$126k
NHLBI NIH HHS F31 HL170755NIGMS NIH HHS R35 GM119412NIGMS NIH HHS R35 GM128666
6 · The paper itself

Abstract

Despite various roles of phosphatidic acid (PA) in cellular functions such as lipid homeostasis and vesicular trafficking, there is a lack of high-affinity tools to study PA in live cells. After analyzing the predicted structure of the LNS2 domain from the lipid transfer protein Nir1, we suspected that this phosphatidic acid-interacting Lipin-like sequence of Nir1 (PILS-Nir1) could serve as a novel PA biosensor. We then performed liposome binding assays as well as pharmacological and genetic manipulations of HEK293A cells expressing a fluorescent PILS-Nir1 to determine how specific lipids affect the interaction of PILS-Nir1 with membranes. We found that PILS-Nir1 bound to both PA and PIP

Identifiers

PMID38464273
PMCPMC10925316
OpenAlexW4392244101

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.