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Gene Review

COX7A2L  -  cytochrome c oxidase subunit VIIa...

Homo sapiens

Synonyms: COX7AR, COX7RP, COX7a-related protein, Cytochrome c oxidase subunit 7A-related protein, mitochondrial, Cytochrome c oxidase subunit VIIa-related protein, ...
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Disease relevance of COX7A2L

  • Then cDNAs associated with two of them, EB1 and EB9, were isolated from libraries of human placenta and MCF-7 cells derived from a human breast cancer, respectively [1].
  • The switch from latent to lytic infection is triggered by the EBV immediate-early transcription factor ZEBRA (BZLF1, Zta, Z, EB1) [2].
  • Characterization of a hemoglobin protease secreted by the pathogenic Escherichia coli strain EB1 [3].
  • The first step in anaerobic ethylbenzene mineralization in denitrifying Azoarcus sp. strain EB1 is the oxidation of ethylbenzene to (S)-(-)-1-phenylethanol [4].
  • The Burkitt lymphoma (BL)-derived, HLA-DR antigen positive B cell line, EB1, is a consistently low stimulator in MLC [5].

High impact information on COX7A2L

  • Moreover, removal of the key flexible tail from EB1 activates microtubule assembly by EB1 alone, suggesting that the flexible tail negatively regulates EB1 activity [6].
  • Here we report the crystal structure of two plus-end complex components, the carboxy-terminal dimerization domain of EB1 and the microtubule binding (CAP-Gly) domain of the dynactin subunit p150Glued [6].
  • Each molecule of the EB1 dimer contains two helices forming a conserved four-helix bundle, while also providing p150Glued binding sites in its flexible tail region [6].
  • Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1- and myosin X-dependent manner [7].
  • Furthermore, myosin X and the microtubule plus-end-tracking protein EB1 are shown to play a role in this mechanism through remodeling of actin cytoskeleton and stabilization of astral microtubules, respectively [7].

Chemical compound and disease context of COX7A2L


Biological context of COX7A2L


Anatomical context of COX7A2L

  • A recently identified third member of the gene family, COX7AR, encodes a protein previously thought to function in mitochondria [12].
  • Structural basis for the activation of microtubule assembly by the EB1 and p150Glued complex [6].
  • Adding another layer of complexity to these interactions, two studies published in this issue implicate EB1 in cross-talk between mitotic MTs and between MTs and actin filaments (Goshima et al., p. 229; Wu et al., p. 201) [13].
  • To view nucleation in living cells, we imaged GFP-tagged EB1, a microtubule tip-binding protein, and determined rates of nucleation by counting the number of EB1-GFP comets emerging from the centrosome over time [10].
  • We show here that domain B is an R-responsive element in HeLa cells and is therefore not an EB1-responsive B-cell-specific element [14].

Associations of COX7A2L with chemical compounds

  • Antibodies raised against a glutathione S-transferase SIG81 fusion protein detected a 13.5-kDa protein that co-fractionates with mitochondrial localized enzymatic activity [9].

Analytical, diagnostic and therapeutic context of COX7A2L

  • Sequence analyses indicate that the duplication of COX7AR occurred prior to the origin of the Euteleostomi (bony vertebrates) and that pCOX7AR is more highly conserved than the two other isoforms [12].
  • Combining crystallography, NMR, and mutational analyses, our studies reveal the critical interacting elements of both EB1 and p150Glued, whose mutation alters microtubule polymerization activity [6].


  1. Isolation of estrogen-responsive genes with a CpG island library. Watanabe, T., Inoue, S., Hiroi, H., Orimo, A., Kawashima, H., Muramatsu, M. Mol. Cell. Biol. (1998) [Pubmed]
  2. Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein. Petosa, C., Morand, P., Baudin, F., Moulin, M., Artero, J.B., Müller, C.W. Mol. Cell (2006) [Pubmed]
  3. Characterization of a hemoglobin protease secreted by the pathogenic Escherichia coli strain EB1. Otto, B.R., van Dooren, S.J., Nuijens, J.H., Luirink, J., Oudega, B. J. Exp. Med. (1998) [Pubmed]
  4. Isolation and characterization of anaerobic ethylbenzene dehydrogenase, a novel Mo-Fe-S enzyme. Johnson, H.A., Pelletier, D.A., Spormann, A.M. J. Bacteriol. (2001) [Pubmed]
  5. Serological distinction between DR antigens and lymphocyte activating determinants. van Heyningen, V., Cohen, B.B., Deane, D.L., Gray, C., Steel, C.M. Tissue Antigens (1981) [Pubmed]
  6. Structural basis for the activation of microtubule assembly by the EB1 and p150Glued complex. Hayashi, I., Wilde, A., Mal, T.K., Ikura, M. Mol. Cell (2005) [Pubmed]
  7. Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1- and myosin X-dependent manner. Toyoshima, F., Nishida, E. EMBO J. (2007) [Pubmed]
  8. In vitro studies on the initial reactions of anaerobic ethylbenzene mineralization. Johnson, H.A., Spormann, A.M. J. Bacteriol. (1999) [Pubmed]
  9. Identification of an additional member of the cytochrome c oxidase subunit VIIa family of proteins. Segade, F., Hurlé, B., Claudio, E., Ramos, S., Lazo, P.S. J. Biol. Chem. (1996) [Pubmed]
  10. Centrosome maturation: measurement of microtubule nucleation throughout the cell cycle by using GFP-tagged EB1. Piehl, M., Tulu, U.S., Wadsworth, P., Cassimeris, L. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  11. Dictyostelium EB1 is a genuine centrosomal component required for proper spindle formation. Rehberg, M., Gräf, R. Mol. Biol. Cell (2002) [Pubmed]
  12. Retention of a duplicate gene through changes in subcellular targeting: an electron transport protein homologue localizes to the golgi. Schmidt, T.R., Doan, J.W., Goodman, M., Grossman, L.I. J. Mol. Evol. (2003) [Pubmed]
  13. TIP maker and TIP marker; EB1 as a master controller of microtubule plus ends. Vaughan, K.T. J. Cell Biol. (2005) [Pubmed]
  14. The Epstein-Barr virus (EBV) ORI1yt enhancer is not B-cell specific and does not respond synergistically to the EBV transcription factors R and Z. Gruffat, H., Moreno, N., Sergeant, A. J. Virol. (1990) [Pubmed]
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