Evidence map›Paper›PMID 41748625›Full record

ArticleNature communications2026

A heteromeric TRP channel that functions as a WNT-activated G protein-coupled receptor.

Emily P Hardy, A Nasim Haider, Maulin M Patel, Vasyl Nesin, Hanh T M Hoang, Sandra E Gostynska, William L Berry, Augen A Pioszak, Mohiuddin Ahmad, Stephen C Parnell and 1 more

Abstract read
In one paragraph

Article in Nature communications, 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

11 authors.

Emily P HardyDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
A Nasim HaiderDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.ORCID http://orcid.org/0000-0002-5675-4560
Maulin M PatelDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
Vasyl NesinDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
Hanh T M HoangDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
Sandra E GostynskaDepartment of Biochemistry and Physiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
William L BerryDepartment of Surgery, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.ORCID http://orcid.org/0000-0002-1661-5443
Augen A PioszakDepartment of Biochemistry and Physiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.
Mohiuddin AhmadDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA.ORCID http://orcid.org/0000-0002-0976-9620
Stephen C ParnellDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS, USA.
Leonidas TsiokasDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA. leonidas-tsiokas@ou.edu.ORCID http://orcid.org/0000-0002-3659-1813

Funding

Polycystin Function Resource Development CoreU54DK126126 · NIDDK · UNIVERSITY OF KANSAS MEDICAL CENTER · PI Alan S Yu · 2020 to 2026
$5.8M
RAMP-altered Class B GPCR Hormone RecognitionR01GM104251 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI PIOSZAK, AUGEN A · 2012 to 2024
$4.2M
Regulation of Oxytocin Receptor Signaling in NeuronsR01MH125998 · NIMH · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI Mohiuddin Ahmad · 2022 to 2026
$1.8M
MECHANISMS DRIVING THE FORMATION OF POST-OPERATIVE PERITONEAL ADHESIONSR35GM142786 · NIGMS · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI BERRY, WILLIAM L · 2021 to 2025
$1.8M
NIDDK NIH HHS U54 DK126126NIGMS NIH HHS R01 GM104251NIMH NIH HHS R01 MH125998U.S. Department of Health & Human Services | NIH | National Institute of Diabetes and Digestive and Kidney Diseases (National Institute of Diabetes & Digestive & Kidney Diseases) F31DK30605U.S. Department of Health & Human Services | NIH | National Institute of Diabetes and Digestive and Kidney Diseases (National Institute of Diabetes & Digestive & Kidney Diseases) R01DK59599U.S. Department of Health & Human Services | NIH | National Institute of Diabetes and Digestive and Kidney Diseases (National Institute of Diabetes & Digestive & Kidney Diseases) U54DK126126U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R01GM104251U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R35GM142786U.S. Department of Health & Human Services | NIH | National Institute of Mental Health (NIMH) R01MH125998
6 · The paper itself

Abstract

The human genome contains approximately 800 G protein-coupled receptors (GPCRs), all characterized by a common 7-transmembrane domain architecture. Here, we show that PKD1, an 11-transmembrane protein with a noncanonical transient receptor potential (TRP) channel architecture, functions as a GPCR with unique biochemical properties. PKD1 acts as a WNT-activated receptor, directly coupling to heterotrimeric Gα

Indexed as

Receptors, G-Protein-CoupledTRPP Cation ChannelsWnt ProteinsAnimalsCell MembraneCyclic AMPHEK293 CellsHumansMutationCyclic AMPReceptors, G-Protein-CoupledTRPP Cation ChannelsWnt Proteins

Identifiers

PMID41748625
PMCPMC13061903

What OpenQuestion 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 OpenQuestion graph.