Evidence map›Paper›PMID 42721955›Full record

ReviewPhysiological reviews2026

Lipid flip-flop in biological membranes: through the lens of TMEM16F.

Ke Z Shan, Augustus J Lowry, Maria A González Torres, Megha S Seri, Huanghe Yang

Abstract readReview
In one paragraph

Review in Physiological reviews, 2026. 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.

No citing paper in PubMed yet.

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

5 authors.

Ke Z ShanDepartment of Biochemistry, Duke University School of Medicine, NC 27710, USA.
Augustus J LowryDepartment of Biochemistry, Duke University School of Medicine, NC 27710, USA.
Maria A González TorresDepartment of Biochemistry, Duke University School of Medicine, NC 27710, USA.
Megha S SeriDepartment of Biochemistry, Duke University School of Medicine, NC 27710, USA.
Huanghe YangDepartment of Biochemistry, Duke University School of Medicine, NC 27710, USA.ORCID 0000-0001-9521-9328

Funding

Advancing mechanistic understanding of membrane ion and lipid transportR35GM153196 · NIGMS · DUKE UNIVERSITY · PI Huanghe Yang · 2024 to 2026
$1.4M
Deciphering mechanobiology in human diseases by developing a TMEM63B channelopathy mouse modelR21OD037849 · OD · DUKE UNIVERSITY · PI YANG, HUANGHE · 2024 to 2025
$426k
HHS | National Institutes of Health (NIH) R21OD037849HHS | National Institutes of Health (NIH) R35GM153196NIGMS NIH HHS R35 GM153196NIH HHS R21 OD037849
6 · The paper itself

Abstract

The asymmetric distribution of phospholipids between membrane leaflets is a hallmark of all known cells, yet many fundamental questions about membrane lipid asymmetry remain unanswered. Why do cells invest energy to establish and maintain this thermodynamically unstable state? How do cells exploit lipid asymmetry to support essential functions? What are the consequences for health and disease when this organization breaks down? Recent identification of bona fide lipid scramblases, which catalyze rapid phospholipid translocation across the hydrophobic membrane core (lipid flip-flop), has shed new light on these longstanding questions. In particular, studies of the Ca²⁺-activated phospholipid scramblase TMEM16F have revealed how regulated lipid scrambling can couple Ca²⁺ signaling to membrane remodeling, phosphatidylserine (PS) exposure, cellular communication, and disease pathogenesis. In this review, we examine the biology of regulated transmembrane phospholipid flip-flop mediated by lipid scramblases, using TMEM16F as a prototypical model to illustrate core molecular mechanisms, physiological functions, pathological implications, and emerging pharmacological opportunities. By placing TMEM16F within the broader landscape of lipid scramblases and scramblase-like proteins, we highlight how regulated membrane lipid scrambling shapes cell physiology and disease. We also discuss critical knowledge gaps and future directions for understanding this rapidly evolving field.

Indexed as

Cell signalingLipid asymmetryPhosphatidylserineScramablasesTMEM16F

Identifiers

PMID42721955
PMCPMC13619121

What OpenQuestion holds

Textmetadata
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.