Mitochondrial proteins at unexpected cellular locations: export of proteins from mitochondria from an evolutionary perspective - PubMed
Review
Mitochondrial proteins at unexpected cellular locations: export of proteins from mitochondria from an evolutionary perspective
B J Soltys et al. Int Rev Cytol. 2000.
Abstract
Researchers in a wide variety of unrelated areas studying functions of different proteins are unexpectedly finding that their proteins of interest are actually mitochondrial proteins, although functions would appear to be extramitochondrial. We review the leading current examples of mitochondrial macromolecules indicated to be also present outside of mitochondria that apparently exit from mitochondria to arrive at their destinations. Mitochondrial chaperones, which have been implicated in growth and development, autoimmune diseases, cell mortality, antigen presentation, apoptosis, and resistance to antimitotic drugs, provide some of the best studied examples pointing to roles for mitochondria and mitochondrial proteins in diverse cellular phenomena. To explain the observations, we propose that specific export mechanisms exist by which certain proteins exit mitochondria, allowing these proteins to have additional functions at specific extramitochondrial sites. Several possible mechanisms by which mitochondrial proteins could be exported are discussed. Gram-negative proteobacteria, from which mitochondria evolved, contain a number of different mechanisms for protein export. It is likely that mitochondria either retained or evolved export mechanisms for certain specific proteins.
Similar articles
-
Gutiérrez T, Simmen T. Gutiérrez T, et al. Cell Calcium. 2018 Mar;70:64-75. doi: 10.1016/j.ceca.2017.05.015. Epub 2017 May 31. Cell Calcium. 2018. PMID: 28619231 Review.
-
Unusual cellular disposition of the mitochondrial molecular chaperones Hsp60, Hsp70 and Hsp10.
Gupta RS, Ramachandra NB, Bowes T, Singh B. Gupta RS, et al. Novartis Found Symp. 2008;291:59-68; discussion 69-73, 137-40. doi: 10.1002/9780470754030.ch5. Novartis Found Symp. 2008. PMID: 18575266
-
Cellular responses to endoplasmic reticulum stress and apoptosis.
Rasheva VI, Domingos PM. Rasheva VI, et al. Apoptosis. 2009 Aug;14(8):996-1007. doi: 10.1007/s10495-009-0341-y. Epub 2009 Apr 10. Apoptosis. 2009. PMID: 19360473 Review.
-
An ER surface retrieval pathway safeguards the import of mitochondrial membrane proteins in yeast.
Hansen KG, Aviram N, Laborenz J, Bibi C, Meyer M, Spang A, Schuldiner M, Herrmann JM. Hansen KG, et al. Science. 2018 Sep 14;361(6407):1118-1122. doi: 10.1126/science.aar8174. Science. 2018. PMID: 30213914
-
Greenberg EF, Vatolin S. Greenberg EF, et al. Rejuvenation Res. 2018 Jun;21(3):225-231. doi: 10.1089/rej.2017.1973. Epub 2017 Sep 25. Rejuvenation Res. 2018. PMID: 28791889
Cited by
-
Batista WL, Matsuo AL, Ganiko L, Barros TF, Veiga TR, Freymüller E, Puccia R. Batista WL, et al. Eukaryot Cell. 2006 Feb;5(2):379-90. doi: 10.1128/EC.5.2.379-390.2006. Eukaryot Cell. 2006. PMID: 16467478 Free PMC article.
-
Alteration of Cpn60 expression in pancreatic tissue of rats with acute pancreatitis.
Li XL, Li K, Li YY, Feng Y, Gong Q, Li YN, Li XJ, Chen CJ. Li XL, et al. Cell Stress Chaperones. 2009 Mar;14(2):199-206. doi: 10.1007/s12192-008-0074-9. Epub 2008 Sep 3. Cell Stress Chaperones. 2009. PMID: 18766470 Free PMC article.
-
Gingrich JR, Pelkey KA, Fam SR, Huang Y, Petralia RS, Wenthold RJ, Salter MW. Gingrich JR, et al. Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):6237-42. doi: 10.1073/pnas.0401413101. Epub 2004 Apr 6. Proc Natl Acad Sci U S A. 2004. PMID: 15069201 Free PMC article.
-
Hu Z, Fan Z, Zhao Z, Chen J, Li J. Hu Z, et al. PLoS One. 2012;7(4):e35542. doi: 10.1371/journal.pone.0035542. Epub 2012 Apr 17. PLoS One. 2012. PMID: 22530046 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Other Literature Sources