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

• Anaerobic mineralization of ethylbenzene by the denitrifying bacterium Azoarcus sp. strain EB1 was recently shown to be initiated by dehydrogenation of ethylbenzene to 1-phenylethanol [8].

Biological context of COX7A2L

• We report the cloning, nucleotide sequence, evolutionary analysis, and intracellular localization of SIG81, a silica-induced cDNA from mouse macrophages [9].
• Southern blot analysis showed that the mouse genome contains two to three copies of the SIG81 gene [9].
• A human SIG81 sequence >80% identical with the mouse cDNA was deducted from homologous sequences in the human expressed tags data base [9].
• Centrosome maturation: measurement of microtubule nucleation throughout the cell cycle by using GFP-tagged EB1 [10].
• EB1 proteins are ubiquitous microtubule-associated proteins involved in microtubule search and capture, regulation of microtubule dynamics, cell polarity, and chromosome stability [11].

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].

References