Evidence map›Paper›PMID 39979596›Full record

ArticleNature methods2025

Genetically encoded biosensor for fluorescence lifetime imaging of PTEN dynamics in the intact brain.

Tomer Kagan, Matan Gabay, Aasha Meenakshisundaram, Yossi Levi, Sharbel Eid, Nikol Malchenko, Maya Maman, Anat Nitzan, Luca Ravotto, Ronen Zaidel-Bar and 3 more

Abstract read
In one paragraph

Article in Nature methods, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

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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

13 authors.

Tomer KaganDepartment of Physiology and Pharmacology, Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv, Israel.
Matan GabayDepartment of Oral Biology, The Goldschleger School of Dental Medicine, Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv, Israel.
Aasha MeenakshisundaramInstitute of Biochemistry and Molecular Biology, Charité Universitätsmedizin Berlin, Berlin, Germany.
Yossi LeviDepartment of Physiology and Pharmacology, Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv, Israel.
Sharbel EidDepartment of Physiology and Pharmacology, Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv, Israel.
Nikol MalchenkoDepartment of Physiology and Pharmacology, Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv, Israel.
Maya MamanDepartment of Physiology and Pharmacology, Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv, Israel.
Anat NitzanDepartment of Cell and Developmental Biology, Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv, Israel.
Luca RavottoInstitute of Pharmacology and Toxicology, University of Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-0431-9866
Ronen Zaidel-BarDepartment of Cell and Developmental Biology, Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv, Israel.
Britta Johanna EickholtInstitute of Biochemistry and Molecular Biology, Charité Universitätsmedizin Berlin, Berlin, Germany.ORCID http://orcid.org/0000-0001-7873-8687
Maayan GalDepartment of Oral Biology, The Goldschleger School of Dental Medicine, Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv, Israel.
Tal LavivDepartment of Physiology and Pharmacology, Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv, Israel. lavivtal@tauex.tau.ac.il.ORCID http://orcid.org/0000-0003-1460-6698

Funding

Israel Science Foundation (ISF) 1384/21, 1385/21
6 · The paper itself

Abstract

The phosphatase and tensin homolog (PTEN) is a vital protein that maintains an inhibitory brake for cellular proliferation and growth. Accordingly, PTEN loss-of-function mutations are associated with a broad spectrum of human pathologies. Despite its importance, there is currently no method to directly monitor PTEN activity with cellular specificity within intact biological systems. Here we describe the development of a FRET-based biosensor using PTEN conformation as a proxy for the PTEN activity state, for two-photon fluorescence lifetime imaging microscopy. We identify a point mutation that allows the monitoring of PTEN activity with minimal interference to endogenous PTEN signaling. We demonstrate imaging of PTEN activity in cell lines, intact Caenorhabditis elegans and in the mouse brain. Finally, we develop a red-shifted sensor variant that allows us to identify cell-type-specific PTEN activity in excitatory and inhibitory cortical cells. In summary, our approach enables dynamic imaging of PTEN activity in vivo with unprecedented spatial and temporal resolution.

Indexed as

Biosensing TechniquesBrainPTEN PhosphohydrolaseAnimalsCaenorhabditis elegansFluorescence Resonance Energy TransferHumansMicePTEN PhosphohydrolasePTEN protein, human

Identifiers

PMID39979596
PMCPMC11978514

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.