ArticleLaboratory investigation; a journal of technical methods and pathology2022
Interactions between leucines within the signal peptides of megalin and stanniocalcin-1 are crucial for regulation of mitochondrial metabolism.
Article in Laboratory investigation; a journal of technical methods and pathology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Endosomes as central hubs of interorganellar communication and cellular homeostasis.Protein & cell · 2026Review
- Receptor-mediated endocytosis by Megalin: Exploring its role in ligand interaction and disease mechanisms.Genes & diseases · 2026Review
- Deletion of Megalin in Kidney Tubular Epithelium Up-Regulates TGFβ1 Signaling, Aggravates Ischemia/Reperfusion Kidney Injury, and Accelerates the Progression to Chronic Kidney Disease.The American journal of pathology · 2026Article
- Stanniocalcin-1: A Novel Mediator in Diabetic Kidney Disease and Cardiovascular Disease.Kidney international reports · 2025Review
- Stanniocalcin Protein Expression in Female Reproductive Organs: Literature Review and Public Cancer Database Analysis.Endocrinology · 2024Review
- Mechanisms of gelofusine protection in an in vitro model of polymyxin B-associated renal injury.American journal of physiology. Renal physiology · 2024Article
- Identification and characterization of a membrane receptor that binds to human STC1.Life science alliance · 2022Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The mitochondrial intracrine Stanniocalcin 1 (STC1) activates mitochondrial anti-oxidant defenses. LRP2 (megalin) shuttles STC1 to the mitochondria through retrograde early endosome-to-Golgi- and Rab32-mediated pathway, and LRP2 KO impairs mitochondrial respiration and glycolysis. We determined STC1-LRP2 interaction domains using HA- and FLAG-tagged fragments of STC1 and LRP2, respectively, co-expressed in HEK293T cells. The trans-membrane domain of LRP2 is required for trafficking to the mitochondria. STC1-FLAG expressed in LRP2 KO cells fails to reach the mitochondria; thus, mitochondrial STC1 is extracellularly-derived via LRP2-mediated trafficking. Tri-leucines L12-14 in LRP2's signal peptide interact with STC1's signal peptide. Mutant LRP2 (L(12-14)A) does not bind STC1, while hSTC1 lacking signal peptide or Leucines L8/9/11 does not bind LRP2. STC1 fails to induce respiration or glycolysis in megalin KO mouse embryonal fibroblasts (MEF) expressing mutant LRP2, while mutant hSTC1 (L8/L9/L11 - > A8/A9/A11) fails to reach the mitochondria or induce respiration and glycolysis in WT MEF. Our data suggest direct regulation of mitochondrial metabolism by extracellular cues and reveal an important role for signal peptides' leucines in protein-protein interactions and mitochondrial biology.
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