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Gene Review

MAPRE2  -  microtubule-associated protein, RP/EB...

Homo sapiens

Synonyms: APC-binding protein EB2, EB1, EB2, End-binding protein 2, Microtubule-associated protein RP/EB family member 2, ...
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Disease relevance of MAPRE2

  • As the expression level of the RP1 gene in activated T cells and a spectrum of tumor-derived cell lines correlates with the proliferative status of the cells, members of the EB1-like gene family may not only be involved in the tumorigenesis of colorectal cancers but may also play a role in the proliferative control of normal cells [1].
  • Overexpression of EB1 in human esophageal squamous cell carcinoma (ESCC) may promote cellular growth by activating beta-catenin/TCF pathway [2].
  • Expression of an EBV activatable early promoter depends on the presence of both EB1 and EB2 [3].
  • Recently we identified the gene responsible for the RP1 form of autosomal dominant retinitis pigmentosa (adRP) at 8q11-12 and found two different nonsense mutations in three families previously mapped to 8q [4].
  • Further studies will determine whether missense changes in the RP1 gene are associated with disease, whether mutations in other regions of RP1 can cause forms of retinal disease other than adRP and whether the background variation in either the mutated or wild-type RP1 allele plays a role in the disease phenotype [4].

Psychiatry related information on MAPRE2

  • A mutation that abolishes upstream stimulatory factor binding, either alone or in combination with the alpha EB1 mutation, reduces basal activity of the promoter to approximately 21% of control levels in alpha T3-1 cells and abolishes the decrease in promoter activity seen when Id is overexpressed [5].

High impact information on MAPRE2

  • Here we have identified two mutations in a novel retina-specific gene from chromosome 8q that cause the RP1 form of autosomal dominant RP in three unrelated families [6].
  • EB1 is located on microtubules of the mitotic spindle and is important in spindle assembly [7].
  • EB1 family proteins may have a general role in linking the microtubule cytoskeleton to cortical polarity determinants [8].
  • Spindles cotton on to junctions, APC and EB1 [9].
  • Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1- and myosin X-dependent manner [10].

Chemical compound and disease context of MAPRE2

  • Although Hafnia alvei was a major component of the Enterobacteriaceae flora in all foods tested and a strong AHL producer, the signal molecules produced by H. alvei strain EB1 did not influence protease production by Pseudomonas fluorescens strain 395 in vitro [11].

Biological context of MAPRE2

  • We also determined that the EB1 family protein-binding regions are amino acids 2781-2820 and 18-111 of APC and p150glued, respectively [12].
  • The rapid up-regulation of RP1 mRNA in properly activated T cells suggests that this gene might belong to the immediate/early gene family, which controls the signal transduction cascade downstream of the TCR [1].
  • The RP1 gene was found to be encoded on chromosome 18q21, a locus which is altered or deleted in up to 50% of all patients with colorectal cancer [13].
  • Data obtained with highly conserved yeast homologues suggest that the EB1/RP1 protein family promotes cytoplasmic microtubule dynamics and contributes to the sensor mechanism controlling the cytokinesis checkpoint during mitosis [13].
  • We report that overexpression of EB1 in the ESCC line EC9706 significantly promotes cell growth, whereas suppression of EB1 protein level by RNA interference significantly inhibited growth of esophageal tumor cells [2].

Anatomical context of MAPRE2


Associations of MAPRE2 with chemical compounds


Physical interactions of MAPRE2


Other interactions of MAPRE2

  • The MAPRE genes encode the EB1 family proteins [22].
  • An unexpected reciprocal cross-inhibition of soluble antigen antibody complex binding was observed between antibodies reacting to distinct determinants, i.e. for NA27 towards NA39/EB2 and for NA71 towards EB1/EB3 [23].
  • 60S APC did not contain EB1 or diaphanous, proteins that have been reported to interact with APC and are implicated in microtubule plus end stabilization [24].
  • EB1 is the first gene on chromosome 20 found to fuse with MLL [25].

Analytical, diagnostic and therapeutic context of MAPRE2


  1. RP1, a new member of the adenomatous polyposis coli-binding EB1-like gene family, is differentially expressed in activated T cells. Renner, C., Pfitzenmeier, J.P., Gerlach, K., Held, G., Ohnesorge, S., Sahin, U., Bauer, S., Pfreundschuh, M. J. Immunol. (1997) [Pubmed]
  2. Overexpression of EB1 in human esophageal squamous cell carcinoma (ESCC) may promote cellular growth by activating beta-catenin/TCF pathway. Wang, Y., Zhou, X., Zhu, H., Liu, S., Zhou, C., Zhang, G., Xue, L., Lu, N., Quan, L., Bai, J., Zhan, Q., Xu, N. Oncogene (2005) [Pubmed]
  3. Both Epstein-Barr virus (EBV)-encoded trans-acting factors, EB1 and EB2, are required to activate transcription from an EBV early promoter. Chevallier-Greco, A., Manet, E., Chavrier, P., Mosnier, C., Daillie, J., Sergeant, A. EMBO J. (1986) [Pubmed]
  4. Mutations in the RP1 gene causing autosomal dominant retinitis pigmentosa. Bowne, S.J., Daiger, S.P., Hims, M.M., Sohocki, M.M., Malone, K.A., McKie, A.B., Heckenlively, J.R., Birch, D.G., Inglehearn, C.F., Bhattacharya, S.S., Bird, A., Sullivan, L.S. Hum. Mol. Genet. (1999) [Pubmed]
  5. Upstream stimulatory factor, a basic-helix-loop-helix-zipper protein, regulates the activity of the alpha-glycoprotein hormone subunit gene in pituitary cells. Jackson, S.M., Gutierrez-Hartmann, A., Hoeffler, J.P. Mol. Endocrinol. (1995) [Pubmed]
  6. Mutations in a novel retina-specific gene cause autosomal dominant retinitis pigmentosa. Sullivan, L.S., Heckenlively, J.R., Bowne, S.J., Zuo, J., Hide, W.A., Gal, A., Denton, M., Inglehearn, C.F., Blanton, S.H., Daiger, S.P. Nat. Genet. (1999) [Pubmed]
  7. A cytokinesis checkpoint requiring the yeast homologue of an APC-binding protein. Muhua, L., Adames, N.R., Murphy, M.D., Shields, C.R., Cooper, J.A. Nature (1998) [Pubmed]
  8. Positioning of the mitotic spindle by a cortical-microtubule capture mechanism. Lee, L., Tirnauer, J.S., Li, J., Schuyler, S.C., Liu, J.Y., Pellman, D. Science (2000) [Pubmed]
  9. Spindles cotton on to junctions, APC and EB1. Bienz, M. Nat. Cell Biol. (2001) [Pubmed]
  10. 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]
  11. Occurrence of proteolytic activity and N-acyl-homoserine lactone signals in the spoilage of aerobically chill-stored proteinaceous raw foods. Liu, M., Gray, J.M., Griffiths, M.W. J. Food Prot. (2006) [Pubmed]
  12. Characterization of functional domains of human EB1 family proteins. Bu, W., Su, L.K. J. Biol. Chem. (2003) [Pubmed]
  13. Chromosomal localization and promoter analysis of the adenomatous polyposis coli binding protein RP1. Wadle, A., Thiel, G., Mischo, A., Jung, V., Pfreundschuh, M., Renner, C. Oncogene (2001) [Pubmed]
  14. CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end dynamics at the cell cortex. Mimori-Kiyosue, Y., Grigoriev, I., Lansbergen, G., Sasaki, H., Matsui, C., Severin, F., Galjart, N., Grosveld, F., Vorobjev, I., Tsukita, S., Akhmanova, A. J. Cell Biol. (2005) [Pubmed]
  15. Regulation of microtubule assembly by human EB1 family proteins. Bu, W., Su, L.K. Oncogene (2001) [Pubmed]
  16. Regulation and function of the interaction between the APC tumour suppressor protein and EB1. Askham, J.M., Moncur, P., Markham, A.F., Morrison, E.E. Oncogene (2000) [Pubmed]
  17. RP1 is required for the correct stacking of outer segment discs. Liu, Q., Lyubarsky, A., Skalet, J.H., Pugh, E.N., Pierce, E.A. Invest. Ophthalmol. Vis. Sci. (2003) [Pubmed]
  18. EB1 targets to kinetochores with attached, polymerizing microtubules. Tirnauer, J.S., Canman, J.C., Salmon, E.D., Mitchison, T.J. Mol. Biol. Cell (2002) [Pubmed]
  19. A role for regulated binding of p150(Glued) to microtubule plus ends in organelle transport. Vaughan, P.S., Miura, P., Henderson, M., Byrne, B., Vaughan, K.T. J. Cell Biol. (2002) [Pubmed]
  20. Disruption of the plasma membrane stimulates rearrangement of microtubules and lipid traffic toward the wound site. Togo, T. J. Cell. Sci. (2006) [Pubmed]
  21. The Epstein-Barr virus (EBV) early protein EB2 is a posttranscriptional activator expressed under the control of EBV transcription factors EB1 and R. Buisson, M., Manet, E., Trescol-Biemont, M.C., Gruffat, H., Durand, B., Sergeant, A. J. Virol. (1989) [Pubmed]
  22. Characterization of human MAPRE genes and their proteins. Su, L.K., Qi, Y. Genomics (2001) [Pubmed]
  23. Study of antigenic structure and inhibition of activity of human growth hormone and chorionic somatomammotropin by monoclonal antibodies. Ivanyi, J. Mol. Immunol. (1982) [Pubmed]
  24. Characterization of a 60S complex of the adenomatous polyposis coli tumor suppressor protein. Mahadevaiyer, S., Xu, C., Gumbiner, B.M. Biochim. Biophys. Acta (2007) [Pubmed]
  25. MLL is fused to EB1 (MAPRE1), which encodes a microtubule-associated protein, in a patient with acute lymphoblastic leukemia. Fu, J.F., Hsu, H.C., Shih, L.Y. Genes Chromosomes Cancer (2005) [Pubmed]
  26. Antigenic, receptor-binding and mitogenic activity of proteolytic fragments of human growth hormone. Aston, R., Ivanyi, J. EMBO J. (1983) [Pubmed]
  27. Interaction of upstream stimulatory factor proteins with an E-box located within the human CYP1A2 5'-flanking gene contributes to basal transcriptional gene activation. Pickwell, G.V., Shih, H., Quattrochi, L.C. Biochem. Pharmacol. (2003) [Pubmed]
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