ArticleThe EMBO journal2013
Structural features within the nascent chain regulate alternative targeting of secretory proteins to mitochondria.
Article in The EMBO journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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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.
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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.
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Who cites it
22 citing papers in PubMed, 38 citations in OpenAlex.
- Rules of Engagement for Components of Membrane Protein Biogenesis at the Human Endoplasmic Reticulum.International journal of molecular sciences · 2025Review
- Leader peptide or pro-segment mutants of renin are misrouted to mitochondria in autosomal dominant tubulointerstitial kidney disease.Disease models & mechanisms · 2023Article
- Signal Peptide Features Determining the Substrate Specificities of Targeting and Translocation Components in Human ER Protein Import.Frontiers in physiology · 2022Review
- Membrane Domain Localization and Interaction of the Prion-Family Proteins, Prion and Shadoo with Calnexin.Membranes · 2021Article
- Quantitative Proteomics and Differential Protein Abundance Analysis after the Depletion of PEX3 from Human Cells Identifies Additional Aspects of Protein Targeting to the ER.International journal of molecular sciences · 2021Article
- Quantitative Proteomics and Differential Protein Abundance Analysis after Depletion of Putative mRNA Receptors in the ER Membrane of Human Cells Identifies Novel Aspects of mRNA Targeting to the ER.Molecules (Basel, Switzerland) · 2021Article
- Recent Advances in Chemical Biology of Mitochondria Targeting.Frontiers in chemistry · 2021Review
- Defective Sec61α1 underlies a novel cause of autosomal dominant severe congenital neutropenia.The Journal of allergy and clinical immunology · 2020Article
- SecY-mediated quality control prevents the translocation of non-gated porins.Scientific reports · 2020Article
- Proteasomal Inhibition Redirects the PrP-Like Shadoo Protein to the Nucleus.Molecular neurobiology · 2019Article
- The signal peptide plus a cluster of positive charges in prion protein dictate chaperone-mediated Sec61 channel gating.Biology open · 2019Article
- Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases.International journal of molecular sciences · 2018Review
- Proteomics reveals signal peptide features determining the client specificity in human TRAP-dependent ER protein import.Nature communications · 2018Article
- Maternal imprinting on cognition markers of wild type and transgenic Alzheimer's disease model mice.Scientific reports · 2018Article
- Article
- The Sec61/SecY complex is inherently deficient in translocating intrinsically disordered proteins.The Journal of biological chemistry · 2017Article
- Regulation of sub-compartmental targeting and folding properties of the Prion-like protein Shadoo.Scientific reports · 2017Article
- Cellular prion protein is present in mitochondria of healthy mice.Scientific reports · 2017Article
- Cotranslational stabilization of Sec62/63 within the ER Sec61 translocon is controlled by distinct substrate-driven translocation events.Molecular cell · 2015Article
- Protein folding as a driving force for dual protein targeting in eukaryotes.Frontiers in molecular biosciences · 2014Review
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein targeting to specified cellular compartments is essential to maintain cell function and homeostasis. In eukaryotic cells, two major pathways rely on N-terminal signal peptides to target proteins to either the endoplasmic reticulum (ER) or mitochondria. In this study, we show that the ER signal peptides of the prion protein-like protein shadoo, the neuropeptide hormone somatostatin and the amyloid precursor protein have the property to mediate alternative targeting to mitochondria. Remarkably, the targeting direction of these signal peptides is determined by structural elements within the nascent chain. Each of the identified signal peptides promotes efficient ER import of nascent chains containing α-helical domains, but targets unstructured polypeptides to mitochondria. Moreover, we observed that mitochondrial targeting by the ER signal peptides correlates inversely with ER import efficiency. When ER import is compromised, targeting to mitochondria is enhanced, whereas improving ER import efficiency decreases mitochondrial targeting. In conclusion, our study reveals a novel mechanism of dual targeting to either the ER or mitochondria that is mediated by structural features within the nascent chain.
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Registered trials
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.