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Gene Review

MAPRE1  -  microtubule-associated protein, RP/EB...

Homo sapiens

Synonyms: APC-binding protein EB1, EB1, End-binding protein 1, Microtubule-associated protein RP/EB family member 1
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Disease relevance of MAPRE1


High impact information on MAPRE1


Chemical compound and disease context of MAPRE1

  • 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 [7].

Biological context of MAPRE1

  • We found that the three MAPRE genes had similar genomic structures but were on different chromosomes [8].
  • EB1 colocalized both to cytoplasmic microtubules in interphase cells and to spindle microtubules during mitosis, with pronounced centrosome staining [3].
  • Mlph is proposed to be a modular protein binding the melanosome-associated protein Rab27a, Myosin Va (MyoVa), actin, and microtubule end-binding protein (EB1), via distinct N-terminal Rab27a-binding domain (R27BD), medial MyoVa-binding domain (MBD), and C-terminal actin-binding domain (ABD), respectively [9].
  • Immunohistochemical analyses reveal a distinct staining pattern during interphase as well as an association of RP1/EB1 with mitotic microtubule structures [10].
  • Monoclonal antibody EB1 has been shown to enhance the actions of hGH on growth and body composition in Snell dwarf mice and to increase food conversion efficiency [11].

Anatomical context of MAPRE1


Associations of MAPRE1 with chemical compounds


Physical interactions of MAPRE1


Co-localisations of MAPRE1

  • Therefore, EB1 appeared to be co-localized and interact with APC on the growing ends of a subset of microtubules [12].

Regulatory relationships of MAPRE1


Other interactions of MAPRE1

  • The MAPRE genes encode the EB1 family proteins [8].
  • Here we characterized a new Pin2/TRF1-interacting protein, EB1, that was originally identified in our yeast two-hybrid screen [15].
  • These findings showed that the APC-EB1 interaction is regulated within cells and is allowed near the ends of microtubules only under restricted conditions [12].
  • CLIP-170 localizes dynamically to growing microtubule plus ends, colocalizing with the dynein activator dynactin and the APC-binding protein EB1 [16].
  • The elongation speed measured using the GFP-tagged end-binding protein-1 exceeded 200 nm/s and was not influenced by MAP-4 [17].


  1. 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]
  2. 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]
  3. The adenomatous polyposis coli-binding protein EB1 is associated with cytoplasmic and spindle microtubules. Berrueta, L., Kraeft, S.K., Tirnauer, J.S., Schuyler, S.C., Chen, L.B., Hill, D.E., Pellman, D., Bierer, B.E. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  4. Marked, transient inhibition of expression of the Epstein-Barr virus latent membrane protein gene in Burkitt's lymphoma cell lines by electroporation. Gahn, T.A., Sugden, B. J. Virol. (1993) [Pubmed]
  5. 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]
  6. Structural insights into the EB1-APC interaction. Honnappa, S., John, C.M., Kostrewa, D., Winkler, F.K., Steinmetz, M.O. EMBO J. (2005) [Pubmed]
  7. 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]
  8. Characterization of human MAPRE genes and their proteins. Su, L.K., Qi, Y. Genomics (2001) [Pubmed]
  9. A coiled-coil domain of melanophilin is essential for Myosin va recruitment and melanosome transport in melanocytes. Hume, A.N., Tarafder, A.K., Ramalho, J.S., Sviderskaya, E.V., Seabra, M.C. Mol. Biol. Cell (2006) [Pubmed]
  10. EB/RP gene family encodes tubulin binding proteins. Juwana, J.P., Henderikx, P., Mischo, A., Wadle, A., Fadle, N., Gerlach, K., Arends, J.W., Hoogenboom, H., Pfreundschuh, M., Renner, C. Int. J. Cancer (1999) [Pubmed]
  11. Monoclonal antibody enhancement of the effects of human growth hormone on growth and body composition in mice. Holder, A.T., Blows, J.A., Aston, R., Bates, P.C. J. Endocrinol. (1988) [Pubmed]
  12. The dynamic behavior of the APC-binding protein EB1 on the distal ends of microtubules. Mimori-Kiyosue, Y., Shiina, N., Tsukita, S. Curr. Biol. (2000) [Pubmed]
  13. Disruption of the plasma membrane stimulates rearrangement of microtubules and lipid traffic toward the wound site. Togo, T. J. Cell. Sci. (2006) [Pubmed]
  14. Posttranslational nitrotyrosination of alpha-tubulin induces cell cycle arrest and inhibits proliferation of vascular smooth muscle cells. Phung, A.D., Soucek, K., Kubala, L., Harper, R.W., Chlo?? Bulinski, J., Eiserich, J.P. Eur. J. Cell Biol. (2006) [Pubmed]
  15. Involvement of the telomeric protein Pin2/TRF1 in the regulation of the mitotic spindle. Nakamura, M., Zhou, X.Z., Kishi, S., Lu, K.P. FEBS Lett. (2002) [Pubmed]
  16. CLIP-170 interacts with dynactin complex and the APC-binding protein EB1 by different mechanisms. Goodson, H.V., Skube, S.B., Stalder, R., Valetti, C., Kreis, T.E., Morrison, E.E., Schroer, T.A. Cell Motil. Cytoskeleton (2003) [Pubmed]
  17. Microtubule-associated protein-4 (MAP-4) inhibits microtubule-dependent distribution of mRNA in isolated neonatal cardiocytes. Scholz, D., McDermott, P., Garnovskaya, M., Gallien, T.N., Huettelmaier, S., DeRienzo, C., Cooper, G. Cardiovasc. Res. (2006) [Pubmed]
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