ATAD3, a vital membrane bound mitochondrial ATPase involved in tumor progression
- 725 Downloads
ATAD3 (ATPase family AAA Domain-containing protein 3) is a mitochondrial membrane bound ATPase whose function has not yet been discovered but its role is essential for embryonic development. The ATAD3 gene has existed since the pluri-cellular organisms with specialized tissues and has remained unique until vertebrates. In primates and human, two other genes have appeared (called ATAD3B and ATAD3C versus ATAD3A the ancestral gene). ATAD3 knock-down in different non-transformed cell lines is associated with drastic changes in the mitochondrial network, inhibition of proliferation and modification of the functional interactions between mitochondria and endoplasmic reticulum. However, the analysis of the cellular properties of ATAD3A and ATAD3B in different human cancer cell lines shows on the contrary that they can present anti-proliferative and chemoresistant properties. ATAD3 may therefore be implicated in an unknown but essential and growth-linked mitochondrial function existing since pluri-cellular organization and involved in tumorigenesis.
KeywordsATAD3 Mitochondria Inner membrane ATPase
Unable to display preview. Download preview PDF.
- Hubstenberger A (2006) MSBP, une protéine identifiée comme une cible de la S100B, impliquée dans la distribution subcellulaire des mitochondries. Thèse de l’Université J. Fourier 2006. http://tel.archives-ouvertes.fr/docs/00/17/52/59/PDF/Arnaud_Hubstenberger.pdf
- He J, Mao CC, Reyes A, Sembongi H, Di Re M, Granycome C, Clippingdale AB, Fearnley IM, Harbour M, Robinson AJ, Reichelt S, Spelbrink JN, Walker JE, Holt IJ (2007) The AAA + protein ATAD3 has displacement loop binding propeties and is involved in mitochondrial nucleoid organization. J Cell Biol 176(2):141–146CrossRefGoogle Scholar
- Smith JS, Alderete B, Minn Y, Borell TJ, Perry A, Mohapatra G, Mohapatra G, Hosek SM, Kimmel D, O’Fallon J, Yates A, Feuerstein BG, Burger PC, Scheithauer BW, Jenkins RB (1999) Localization of common deletion regions on 1p and 19q in human glioma and their association with histological subtype. Oncogene 18:4144–4152CrossRefGoogle Scholar
- Gires O, Münz M, Schaffrik M, Kieu C, Rauch J, Ahlemann M, Eberle D, Mack B, Wollenberg B, Lang S, Hofmann T, Hammerschmidt W, Zeidler R (2004) Profile identification of disease-associated humoral antigens using AMIDA, a novel proteomics-based technology. Cell Mol Life Sci 61(10):1198–207CrossRefGoogle Scholar
- Gilquin B, Cannon BR, Hubstenberger A, Moulouel B, Falk E, Merle N, Assard N, Kieffer S, Rousseau D, Wilder PT, Weber DJ, Baudier J (2010b) The calcium-dependent interaction between S100B and the mitochondrial AAA-ATPase ATAD3A and the role of this complex in the cytoplasmic processing of ATAD3A. Mol Cell Biol 30(11):2724–36CrossRefGoogle Scholar
- Fang HY, Chang CL, Hsu SH, Huang CY, Chiang SF, Chiou SH, Huang CH, Hsiao YT, Lin TY, Chiang IP, Hsu WH, Sugano S, Chen CY, Lin CY, Ko WJ, Chow KC (2010) ATPase family AAA domain-containing 3A is a novel anti-apoptotic factor in lung adenocarcinoma cells. J Cell Sci 123(7):1171–80CrossRefGoogle Scholar
- Kornmann B (2010) Le complexe ERMES : une connexion haut débit entre le réticulum endoplasmique et les mitochondries. Médecine/Science (2)Google Scholar