Translocation of Proteins into Mitochondria

By N. Hoogenraad, M. Ryan. IUBMB Life - A Journal of the International Union of Biochemistry and Molecular Biology, 2001

781 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/399949f6e2dc9c02c9562448c9c963c6929df234

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cellular and Molecular Neuroscience

1. Debashish Chowdhury
2. B. Westermann
3. Eugene V. Koonin
4. S. Jin
5. R. Youle
6. J. Nunnari
7. M. Giezen

In Molecular Biology

1. B. Westermann
2. R. Youle
3. A. Suomalainen
4. J. Nunnari
5. Koji Yamano
6. S. Jin
7. Eugene V. Koonin
8. G. Shadel

Citations in the corpus

• Mitochondrial protein import: from proteomics to functional mechanisms (2010, neutral): “folding of many intermembrane space proteins (5).”
• Mitochondria: In Sickness and in Health (2012, background): “Membrane potential is harnessed for other essential mitochondrial functions, such as mitochondrial protein import (Neupert and Herrmann, 2007), and is used to trigger changes on the molecular level that alter mitochondrial behaviors in response to mitochondrial dysfunction.”
• Whole cell 3D STORM reveals interactions between cellular structures with nanometer-scale resolution (2008, neutral): “We stained Tom20, a component of the translocase of the outer mitochondrial membrane complex and a commonly used mitochondrial outer membrane marke”
• Hydrogenosomes and Mitosomes: Conservation and Evolution of Functions (2009, background): “To this end, nuclear-encoded proteins destined for the mitochondrion need to be imported (see Neupert and Herrmann (2007) for extensive information gleaned from studies on yeast).”
• The Logic of Chance: The Nature and Origin of Biological Evolution (2011, background): “This is yet another “lucky coincidence,” but it is not as unlikely as it might seem because the import peptides are typically simple, repetitive sequences that could evolve by sheer chance (Neupert and Herrmann, 2007).”
• PINK1- and Parkin-mediated mitophagy at a glance (2012, background): “…through the TOM complex and the translocase of inner mitochondrial membrane (TIM) complex, and then released to span the inner mitochondrial membrane (IMM) with its transmembrane (TM) domain acting as a stop transfer signal (Poster Panel 2, upper part) (reviewed by Neupert and Herrmann, 2007).”
• The amyloid β-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae (2008, background): “Targeting signals are first recognized by receptors of TOM, Tom20, Tom22 and Tom70 (26, 27).”
• Importing Mitochondrial Proteins: Machineries and Mechanisms (2009, background): “These precursor proteins are also thought to be translocated in a loop formation (Neupert and Herrmann, 2007).”
• Stochastic mechano-chemical kinetics of molecular motors: A multidisciplinary enterprise from a physicist’s perspective (2012, background): “Do the proteins cross the space between the two membranes of a mitochondrion without active assistance of the translocation machinery? If not, how do the TOM and TIM (and, similarly, TOC and TIC) cooperate to import proteins [1298, 1299, 1300, 1301, 1302, 1303]? Moreover, how are the proteins transl”
• Mitochondrial fusion and fission in cell life and death (2010, background): “Mitochondrial biogenesis involves the import of nucleus-encoded proteins from the cytosol, the incorporation of mitochondrion-synthesized and imported membrane lipids, the amplification of the mitochondrial genome and the translation of mitochondrion-encoded protein”
• Mitochondria in innate immune responses (2011, background): “TOM20 and TOM70 serve as the primary pre-protein receptors and are anchored to the OMM via N-terminal transmembrane segments, whereas the hydrophilic domains of these proteins face the cytosol and bind mitochondrial targeting sequences (MTSs”
• PINK1 is degraded through the N-end rule pathway (2013, background): “Furthermore, PINK1(1-155)-YFP, a mutant with an N-end stabilizing residue was stably localized in the cytosol (Fig.”