ArticleThe EMBO journal1998
Unfolding of preproteins upon import into mitochondria.
Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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.
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.
Who cites it
34 citing papers in PubMed, 99 citations in OpenAlex.
- OMA1 protease eliminates arrested protein import intermediates upon mitochondrial depolarization.The Journal of cell biology · 2024Article
- Cytosolic Quality Control of Mitochondrial Protein Precursors-The Early Stages of the Organelle Biogenesis.International journal of molecular sciences · 2021Review
- Signaling and Regulation of the Mitochondrial Unfolded Protein Response.Cold Spring Harbor perspectives in biology · 2019Review
- Role of the membrane potential in mitochondrial protein unfolding and import.Scientific reports · 2019Article
- Tom70 enhances mitochondrial preprotein import efficiency by binding to internal targeting sequences.The Journal of cell biology · 2018Article
- PINK1 import regulation; a fine system to convey mitochondrial stress to the cytosol.BMC biology · 2018Review
- The ubiquitin signal and autophagy: an orchestrated dance leading to mitochondrial degradation.EMBO reports · 2016Review
- Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015Review
- PINK1 is degraded through the N-end rule pathway.Autophagy · 2013Article
- Dissecting stop transfer versus conservative sorting pathways for mitochondrial inner membrane proteins in vivo.The Journal of biological chemistry · 2013Article
- A model system for mitochondrial biogenesis reveals evolutionary rewiring of protein import and membrane assembly pathways.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Role of the AAA protease Yme1 in folding of proteins in the intermembrane space of mitochondria.Molecular biology of the cell · 2012Article
- Lateral release of proteins from the TOM complex into the outer membrane of mitochondria.The EMBO journal · 2011Article
- Cardiomyopathy of Friedreich's ataxia: use of mouse models to understand human disease and guide therapeutic development.Pediatric cardiology · 2011Article
- Common ground for protein translocation: access control for mitochondria and chloroplasts.Nature reviews. Molecular cell biology · 2011Review
- Efficient mitochondrial targeting relies on co-operation of multiple protein signals in plants.Journal of experimental botany · 2009Article
- TAT opens the door.Molecular therapy : the journal of the American Society of Gene Therapy · 2008Article
- A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import.Molecular and cellular biology · 2007Article
- Characterization of Mmp37p, a Saccharomyces cerevisiae mitochondrial matrix protein with a role in mitochondrial protein import.Molecular biology of the cell · 2006Article
- On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60.Cell stress & chaperones · 2006Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Unfolding of preproteins and translocation across the mitochondrial membranes requires their interaction with mt-Hsp70 and Tim44 at the inner face of the inner membrane and ATP as an energy source. We measured the temperature dependence of the rates of unfolding and import into the matrix of two folded passenger domains, the tightly folded heme-binding domain (HBD) of cytochrome b2 and the loosely folded mouse dihydrofolate reductase (DHFR). Despite the stability of the HBD, its rates of thermal breathing were fast and the preprotein was imported rapidly at all temperatures. In contrast, rates of unfolding and import of DHFR were strongly temperature dependent and import was significantly slower than unfolding. In addition, import rates of DHFR were strongly dependent on the length of the presequence. We propose that the mitochondrial import motor does not exert a constant pulling force. Rather, mt-Hsp70 appears to release a translocating polypeptide chain such that the precursor can then slide back and refold on the surface of the mitochondria. Refolding competes with translocation, and passengers may undergo several rounds of unfolding and refolding prior to their import.
Indexed as
Identifiers
What OpenQuestion holds
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.