Literature DB >> 15157495

Mechanisms of protein import across the mitochondrial outer membrane.

R Lill1, W Neupert.   

Abstract

Mitochondria import the majority of their proteins from the cytosol. At the mitochondrial outer membrane, import is initiated through a series of reactions, which include preprotein recognition, unfolding, insertion and translocation. These processes are facilitated by a multisubunit complex, the TOM complex. Specific roles can now be assigned to several components of this complex. Although the import machinery of the outer membrane can insert and translocate a few proteins on its own, completion of translocation o f most preproteins is dependent upon coupling to both the membrane potential and mt-Hsp70/ATP-driven transport across the inner membrane, mediated by the TIM complex.

Entities:  

Year:  1996        PMID: 15157495     DOI: 10.1016/0962-8924(96)81015-4

Source DB:  PubMed          Journal:  Trends Cell Biol        ISSN: 0962-8924            Impact factor:   20.808


  34 in total

1.  An internal targeting signal directing proteins into the mitochondrial intermembrane space.

Authors:  K Diekert; G Kispal; B Guiard; R Lill
Journal:  Proc Natl Acad Sci U S A       Date:  1999-10-12       Impact factor: 11.205

2.  Nascent polypeptide-associated complex stimulates protein import into yeast mitochondria.

Authors:  U Fünfschilling; S Rospert
Journal:  Mol Biol Cell       Date:  1999-10       Impact factor: 4.138

3.  Apocytochrome c requires the TOM complex for translocation across the mitochondrial outer membrane.

Authors:  K Diekert; A I de Kroon; U Ahting; B Niggemeyer; W Neupert; B de Kruijff; R Lill
Journal:  EMBO J       Date:  2001-10-15       Impact factor: 11.598

4.  Mitochondrial protein import: recognition of internal import signals of BCS1 by the TOM complex.

Authors:  Tincuta Stan; Jan Brix; Jens Schneider-Mergener; Nikolaus Pfanner; Walter Neupert; Doron Rapaport
Journal:  Mol Cell Biol       Date:  2003-04       Impact factor: 4.272

5.  The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44.

Authors:  P J Dekker; F Martin; A C Maarse; U Bömer; H Müller; B Guiard; M Meijer; J Rassow; N Pfanner
Journal:  EMBO J       Date:  1997-09-01       Impact factor: 11.598

6.  Role of the negative charges in the cytosolic domain of TOM22 in the import of precursor proteins into mitochondria.

Authors:  F E Nargang; D Rapaport; R G Ritzel; W Neupert; R Lill
Journal:  Mol Cell Biol       Date:  1998-06       Impact factor: 4.272

7.  Dynamics of the TOM complex of mitochondria during binding and translocation of preproteins.

Authors:  D Rapaport; K P Künkele; M Dembowski; U Ahting; F E Nargang; W Neupert; R Lill
Journal:  Mol Cell Biol       Date:  1998-09       Impact factor: 4.272

Review 8.  Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: implications for cellular function and mitochondrial structure.

Authors:  O Stachowiak; U Schlattner; M Dolder; T Wallimann
Journal:  Mol Cell Biochem       Date:  1998-07       Impact factor: 3.396

9.  Role of the intermembrane-space domain of the preprotein receptor Tom22 in protein import into mitochondria.

Authors:  D A Court; F E Nargang; H Steiner; R S Hodges; W Neupert; R Lill
Journal:  Mol Cell Biol       Date:  1996-08       Impact factor: 4.272

10.  The intermembrane space domain of mitochondrial Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences.

Authors:  M Moczko; U Bömer; M Kübrich; N Zufall; A Hönlinger; N Pfanner
Journal:  Mol Cell Biol       Date:  1997-11       Impact factor: 4.272

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