Tom5 functionally links mitochondrial preprotein receptors to the general import pore-Reference-Cited by-同舟云学术

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Tom5 functionally links mitochondrial preprotein receptors to the general import pore

Published:1997-07 Issue:6638 Volume:388 Page:195-200
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Dietmeier Klaus,Hönlinger Angelika,Bömer Ulf,Dekker Peter J. T.,Eckerskorn Christoph,Lottspeich Fritz,Kübrich Michael,Pfanner Nikolaus

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/40663.pdf

Reference30 articles.

1. Schatz, G. & Dobberstein, B. Common principles of protein translocation across membranes. Science 271, 1519–1526 (1996).

2. Pfanner, N. & Meijer, M. Mitochondrial biogenesis: the Tom and Tim machine. Curr. Biol. 7, R100–R103 (1997).

3. Lill, R. & Neupert, W. Mechanisms of protein import across the mitochondrial outer membrane. Trends Cell Biol. 6, 56–61 (1996).

4. Bolliger, L., Junne, T., Schatz, G. & Lithgow, T. Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria. EMBO J. 14, 6318–6326 (1995).

5. Hönlinger, A. et al. The mitochondrial receptor complex: Mom22 is essential for cell viability and directly interacts with preproteins. Mol. Cell. Biol. 15, 3382–3389 (1995).

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2. The architecture of substrate-engaged TOM–TIM23 supercomplex reveals preprotein proximity sites for mitochondrial protein translocation;Cell Discovery;2024-02-16

3. Interactions of amyloidogenic proteins with mitochondrial protein import machinery in aging-related neurodegenerative diseases;Frontiers in Physiology;2023-11-02

4. Two conformations of the Tom20 preprotein receptor in the TOM holo complex;Proceedings of the National Academy of Sciences;2023-08-14

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