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Gene Review

TIM23  -  protein transporter TIM23

Saccharomyces cerevisiae S288c

Synonyms: MAS6, MIM23, MPI3, Membrane import machinery protein MIM23, Mitochondrial import inner membrane translocase subunit TIM23, ...
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High impact information on MAS6


Biological context of MAS6


Anatomical context of MAS6

  • Two intermembrane space TIM complexes interact with different domains of Tim23p during its import into mitochondria [5].
  • Tim23 import intermediates could also be cross-linked to the complex, suggesting a dual role for the Tim8-Tim13 intermembrane space complex in the import of proteins found in both the outer and inner mitochondrial membranes [9].
  • Tim23p is a mitochondrial inner membrane protein essential for the import of proteins from the cytosol [10].

Associations of MAS6 with chemical compounds

  • In contrast to precursors with an NH2-terminal targeting presequence that are imported in a linear NH2-terminal manner, we show that Tim23p crosses the outer membrane as a loop before inserting into the inner membrane [11].

Physical interactions of MAS6

  • We suggest that Tim50 plays a crucial role in the transfer of preproteins from the TOM complex to the TIM23 complex through the intermembrane space [7].
  • In particular, import of nuclear-encoded precursor proteins into and across the mitochondrial inner membrane is mediated by two distinct translocases, the TIM23 complex and the TIM22 complex [12].
  • Although Tam41 is not a constituent of the TIM23 complex, depletion of Tam41 led to a decreased molecular size of the TIM23 complex and partial aggregation of Pam18 and -16 [13].
  • Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules [10].
  • The purified C-terminal domain of Tim21 appears not to bind to any of the TIM23 components but rather specifically interacts with the TOM complex [14].

Regulatory relationships of MAS6

  • On the basis of these observations we propose that charged residues in Tim17 are critical for the preprotein-induced gating of the TIM23 translocase [15].

Other interactions of MAS6

  • Precursor proteins carrying amino-terminal targeting signals are translocated into the matrix by the integral inner membrane proteins Tim23 and Tim17 in cooperation with Tim44 and mitochondrial Hsp70 [16].
  • We now show that the two 70 kDa complexes each mediate the import of a different subset of integral inner membrane proteins and that they can transfer these proteins to one of three different membrane insertion sites: the TIM22 complex, the TIM23 complex or an as yet uncharacterized insertion site [17].
  • Tim18p does not cofractionate with the TIM23 complex upon immunoprecipitation or nondenaturing gel electrophoresis [18].
  • Conserved N-terminal negative charges in the Tim17 subunit of the TIM23 translocase play a critical role in the import of preproteins into mitochondria [15].
  • PiC thus appears to have a latent signal for sorting to the TIM23 pathway, which is exposed by reduced interactions with the Tim9-Tim10 complex and maintenance of the import competence [19].

Analytical, diagnostic and therapeutic context of MAS6


  1. Mitochondrial presequence translocase: switching between TOM tethering and motor recruitment involves Tim21 and Tim17. Chacinska, A., Lind, M., Frazier, A.E., Dudek, J., Meisinger, C., Geissler, A., Sickmann, A., Meyer, H.E., Truscott, K.N., Guiard, B., Pfanner, N., Rehling, P. Cell (2005) [Pubmed]
  2. The mitochondrial presequence translocase: an essential role of Tim50 in directing preproteins to the import channel. Geissler, A., Chacinska, A., Truscott, K.N., Wiedemann, N., Brandner, K., Sickmann, A., Meyer, H.E., Meisinger, C., Pfanner, N., Rehling, P. Cell (2002) [Pubmed]
  3. Tim23 links the inner and outer mitochondrial membranes. Donzeau, M., Káldi, K., Adam, A., Paschen, S., Wanner, G., Guiard, B., Bauer, M.F., Neupert, W., Brunner, M. Cell (2000) [Pubmed]
  4. Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria. Bauer, M.F., Sirrenberg, C., Neupert, W., Brunner, M. Cell (1996) [Pubmed]
  5. Two intermembrane space TIM complexes interact with different domains of Tim23p during its import into mitochondria. Davis, A.J., Sepuri, N.B., Holder, J., Johnson, A.E., Jensen, R.E. J. Cell Biol. (2000) [Pubmed]
  6. Tom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteins. Gabriel, K., Egan, B., Lithgow, T. EMBO J. (2003) [Pubmed]
  7. Tim50, a novel component of the TIM23 preprotein translocase of mitochondria. Mokranjac, D., Paschen, S.A., Kozany, C., Prokisch, H., Hoppins, S.C., Nargang, F.E., Neupert, W., Hell, K. EMBO J. (2003) [Pubmed]
  8. The import motor of the yeast mitochondrial TIM23 preprotein translocase contains two different J proteins, Tim14 and Mdj2. Mokranjac, D., Sichting, M., Popov-Celeketić, D., Berg, A., Hell, K., Neupert, W. J. Biol. Chem. (2005) [Pubmed]
  9. The Tim8-Tim13 complex of Neurospora crassa functions in the assembly of proteins into both mitochondrial membranes. Hoppins, S.C., Nargang, F.E. J. Biol. Chem. (2004) [Pubmed]
  10. Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules. Ryan, K.R., Leung, R.S., Jensen, R.E. Mol. Cell. Biol. (1998) [Pubmed]
  11. The role of the Tim8p-Tim13p complex in a conserved import pathway for mitochondrial polytopic inner membrane proteins. Curran, S.P., Leuenberger, D., Schmidt, E., Koehler, C.M. J. Cell Biol. (2002) [Pubmed]
  12. Import of proteins into mitochondria: a novel pathomechanism for progressive neurodegeneration. Bauer, M.F., Neupert, W. J. Inherit. Metab. Dis. (2001) [Pubmed]
  13. Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria. Tamura, Y., Harada, Y., Yamano, K., Watanabe, K., Ishikawa, D., Ohshima, C., Nishikawa, S., Yamamoto, H., Endo, T. J. Cell Biol. (2006) [Pubmed]
  14. Role of Tim21 in mitochondrial translocation contact sites. Mokranjac, D., Popov-Celeketić, D., Hell, K., Neupert, W. J. Biol. Chem. (2005) [Pubmed]
  15. Conserved N-terminal negative charges in the Tim17 subunit of the TIM23 translocase play a critical role in the import of preproteins into mitochondria. Meier, S., Neupert, W., Herrmann, J.M. J. Biol. Chem. (2005) [Pubmed]
  16. Carrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5. Sirrenberg, C., Endres, M., Fölsch, H., Stuart, R.A., Neupert, W., Brunner, M. Nature (1998) [Pubmed]
  17. Different import pathways through the mitochondrial intermembrane space for inner membrane proteins. Leuenberger, D., Bally, N.A., Schatz, G., Koehler, C.M. EMBO J. (1999) [Pubmed]
  18. Tim18p, a new subunit of the TIM22 complex that mediates insertion of imported proteins into the yeast mitochondrial inner membrane. Koehler, C.M., Murphy, M.P., Bally, N.A., Leuenberger, D., Oppliger, W., Dolfini, L., Junne, T., Schatz, G., Or, E. Mol. Cell. Biol. (2000) [Pubmed]
  19. The phosphate carrier has an ability to be sorted to either the TIM22 pathway or the TIM23 pathway for its import into yeast mitochondria. Yamano, K., Ishikawa, D., Esaki, M., Endo, T. J. Biol. Chem. (2005) [Pubmed]
  20. Control of mitochondrial protein import by pH. Grigoriev, S.M., Jensen, R.E., Kinnally, K.W. FEBS Lett. (2003) [Pubmed]
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