Evidence map›Paper›PMID 41129951›Full record

ArticleJournal of inorganic biochemistry2026

Progesterone receptor membrane component 1 (PGRMC1) regulates Heme trafficking through mitochondria-ER junctions.

Robert B Piel Iii, Chibuike D Obi, Martonio Ponte Viana, Mathilda M Willoughby, Osiris Martinez-Guzman, Aaliyah Wadley, Yasaman Jami-Alahmadi, James A Wohlschlegel, Kevin G Hicks, Jared Rutter and 6 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of inorganic biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Article
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

16 authors.

Robert B Piel IiiDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
Chibuike D ObiDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
Martonio Ponte VianaDepartment of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA.
Mathilda M WilloughbySchool of Chemistry and Biochemistry and School of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332, USA.
Osiris Martinez-GuzmanSchool of Chemistry and Biochemistry and School of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332, USA.
Aaliyah WadleySchool of Chemistry and Biochemistry and School of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332, USA.
Yasaman Jami-AlahmadiDepartment of Biological Chemistry, University of California, Los Angeles, CA 90095, USA.
James A WohlschlegelDepartment of Biological Chemistry, University of California, Los Angeles, CA 90095, USA.
Kevin G HicksDepartment of Biochemistry University of Utah School of Medicine, Salt Lake City, UT 84112, USA; Department of Nutrition and Integrative Physiology, University of Utah College of Health, Salt Lake City, UT 84112, USA.
Jared RutterDepartment of Biochemistry University of Utah School of Medicine, Salt Lake City, UT 84112, USA; Howard Hughes Medical Institute, University of Utah School of Medicine, Salt Lake City, UT 84112, USA.
J Alan MaschekDepartment of Nutrition and Integrative Physiology, University of Utah College of Health, Salt Lake City, UT 84112, USA; Metabolomics Core Research Facility, University of Utah, Salt Lake City, UT 84112, USA.
J Leon CatrowMetabolomics Core Research Facility, University of Utah, Salt Lake City, UT 84112, USA.
James CoxDepartment of Biochemistry University of Utah School of Medicine, Salt Lake City, UT 84112, USA; Metabolomics Core Research Facility, University of Utah, Salt Lake City, UT 84112, USA.
Amit R ReddiSchool of Chemistry and Biochemistry and School of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332, USA; Parker Petit Institute for Bioengineering and Biosciences, Georgia Institute of Technology, Atlanta, GA 30332, USA.
Oleh KhalimonchukDepartment of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA; Nebraska Redox Biology Center, University of Nebraska, Lincoln, NE 68588, USA; Fred & Pamela Buffett Cancer Center, Omaha, NE 68198, USA.
Amy E MedlockDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA; Department of Interdisciplinary Biomedical Sciences, University of Georgia School of Medicine, Athens, GA 30602, USA. Electronic address: medlock@uga.edu.

Funding

Proteomics CoreU54DK110858 · NIDDK · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Anna E Beaudin, JAMES Eric COX · 2016 to 2026
$8.6M
Mitochondrial Fidelity and HomeostasisR35GM131701 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI Oleh Khalimonchuk · 2019 to 2026
$2.4M
Illuminating Heme Trafficking and Signaling Pathways in Health and DiseaseR35GM145350 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI Amit Ram Reddi · 2022 to 2026
$1.9M
Identifying the Function of the Mitochondrial Heme Biosynthesis Complex in ErythropoiesisR01DK111653 · NIDDK · UNIVERSITY OF GEORGIA · PI MEDLOCK, AMY ELIZABETH · 2017 to 2018
$450k
NIDDK NIH HHS R01 DK111653NIDDK NIH HHS U54 DK110858NIGMS NIH HHS R35 GM131701NIGMS NIH HHS R35 GM145350
6 · The paper itself

Abstract

Heme is a cofactor essential for a multitude of biological reactions. The terminal step of heme synthesis occurs in the mitochondrial matrix which means that heme must be trafficked from there to other locales in the cell. Thus, identifying intracellular heme chaperones is crucial to understanding regulation of global cellular metabolism. The heme-binding protein progesterone receptor membrane component 1 (PGRMC1) has been proposed to function as a chaperone for several biologically active molecules including heme, but its cellular role is not fully understood. Here, we investigate the function of PGRMC1 in heme metabolism. By monitoring intracellular heme location and concentrations in Saccharomyces cerevisiae, we show that mutants lacking damage associated protein 1 (Dap1), the yeast ortholog of PGRMC1, have altered nuclear heme trafficking which can be corrected by complementation with DAP1 or PGRMC1. Biochemical analyses reveal that PGRMC1 co-localizes with known mitochondrial-associated membrane (MAM) proteins and proteomic comparison of interaction partners shows enrichment of MAM-associated proteins and pathways. Metabolomics profiling of wild-type and PGRMC1 knockout cells identifies significant changes of several metabolites, including heme, several amino acids, long chain acyl-carnitine, ethanolamine phosphate, and mevalonic acid. Together, these results provide evidence that PGRMC1 is involved in heme trafficking and homeostasis through MAMs.

Indexed as

Endoplasmic ReticulumHemeMembrane ProteinsMitochondriaReceptors, ProgesteroneSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHemeMembrane ProteinsReceptors, ProgesteroneSaccharomyces cerevisiae ProteinsFerrochelataseHemeMAMsMitochondriaPGRMC1

Identifiers

PMID41129951
PMCPMC12973532

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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.