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MAPRE1 (Microtubule-associated protein, RP/EB family, member 1)

Written2004-11Jennifer S Tirnauer
Center for Molecular Medicine, University of Connecticut Health Center, 263 Farmington Avenue, E1032, Farmington, CT 06030-3101, USA

(Note : for Links provided by Atlas : click)


Other aliasEB1
LocusID (NCBI) 22919
Atlas_Id 455
Location 20q11.21  [Link to chromosome band 20q11]
Location_base_pair Starts at and ends at bp from pter
  EB1-GFP fluorescence on polymerizing microtubule plus ends in a living PtK1 cell.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
ABLIM1 (10q25.3) / MAPRE1 (20q11.21)ENO1 (1p36.23) / MAPRE1 (20q11.21)KMT2A (11q23.3) / MAPRE1 (20q11.21)
MAPRE1 (20q11.21) / KMT2A (11q23.3)MAPRE1 (20q11.21) / MAPRE1 (20q11.21)MAPRE1 (20q11.21) / TM9SF4 (20q11.21)
Note The original name EB1 came from a yeast two hybrid screen "End Binding 1" is a nickname that was later applied when the protein was found to target to microtubule plus ends.


Description 22 Kb genomic locus, 5 introns
Transcription 2540 bp open reading frame


Description 268 amino acids; 35 kDa; EB1 was cloned in yeast two-hybrid screen as binding partner for the tumor suppressor APC (Adenomatous Polyposis Coli); EB1 is a microtubule plus end tracking protein (+tip). It contains a calponin homology domain and a leucine zipper
Expression EB1 is ubiquitously expressed. Protein levels remain similar throughout the cell cycle.
Localisation EB1 targets to the plus ends of microtubules when they are polymerizing, producing a "comet tail" pattern. (Figure 1). The mechanism is treadmilling, in which new subunits are continually added at the tip. EB1 also shows additional weak binding to the microtubule lattice (along the length of the microtubule). EB1 targets to kinetochores moving anti-poleward. This is suspected to be due to binding to kinetochore microtubule plus ends rather than the kinetochore itself. Through its carboxyl terminus, EB1 localizes to centrosomes and spindle poles.
  • The primary function identified to date is regulation of microtubule dynamic instability. Microtubules dynamically convert between growth (polymerization) and shrinkage (depolymerization). The transition from growth to shrinkage is called catastrophe, while the conversion from shrinkage to growth is called rescue. Microtubules also pause in their polymerization. EB1 reduces these pauses and reduces the frequency of catastrophes. EB1 increases the frequency of rescues. The net result is more stable, longer microtubules. This effect is predominantly seen during mitosis.
  • EB1 is important in maintaining the structure of the mitotic spindle. This is thought to be mediated by its effects on spindle microtubule dynamic instability.
  • EB1 is important in spindle positioning within the cell. This is thought to be due to its effects on astral microtubule dynamic instability. In budding yeast, EB1 also plays a role in positioning the mitotic spindle through the bud neck. In this case, it is through microtubule dynamics as well direct binding to a protein at the bud tip, creating a physical link between the microtubule end and the cell cortex.
  • EB1 plays a role in linking kinetochores to kinetochore microtubules, which is important for chromosome stability. It is not known whether it regulates kinetochore microtubule dynamics or end-on attachment.
  • EB1 also has an independent role in anchoring microtubule minus ends to centrosomes
  • Protein-protein interactions: Adenomatous Polyposis Coli (APC) tumor suppressor, polymerized tubulin (microtubules), p150glued/dynactin, CLIP-170, mDia, Pin2/TRF1, RhoGEF2 (drosophila), shortstop (drosophila)
  • Homology MAPRE2, MAPRE3


    Note none known

    Implicated in

    Entity Colon cancer
    Disease Truncation of the Adenomatous Polyposis Coli (APC) protein is seen in Familial Adenomatous Polyposis (FAP) as well as most sporadic colon cancers. EB1 binds to the APC C-terminus, so its binding is lost in most truncations. Also lost are other APC binding partners including the transcription factor beta-catenin. The role of APC as a tumor suppressor is thought to be through the beta-catenin pathway. Some evidence in the mouse suggests that this is true.
    However, there is increasing evidence that connections between APC and the cytoskeleton are important in cell migration, which could have an important role in colon cancer. One Italian FAP family has been reported in which APC is truncated distal to the beta-catenin binding site but including the EB1 binding site. There is no direct evidence of EB1 mutation in colon cancer, and a single report found no evidence of somatic mutations by reverse transcriptase single-strand conformational polymorphism (SSCP) analysis in 21 sporadic colorectal cancers and seven colorectal adenomas.
    Entity Meduloblastoma
    Disease A single report showed that EB1 is transcriptionally elevated in pediatric meduloblastoma. There is no direct evidence of EB1 mutation in meduloblastoma.


    Note none known


    Regulation and function of the interaction between the APC tumour suppressor protein and EB1.
    Askham JM, Moncur P, Markham AF, Morrison EE
    Oncogene. 2000 ; 19 (15) : 1950-1958.
    PMID 10773885
    Evidence that an interaction between EB1 and p150(Glued) is required for the formation and maintenance of a radial microtubule array anchored at the centrosome.
    Askham JM, Vaughan KT, Goodson HV, Morrison EE
    Molecular biology of the cell. 2002 ; 13 (10) : 3627-3645.
    PMID 12388762
    Dissecting interactions between EB1, microtubules and APC in cortical clusters at the plasma membrane.
    Barth AI, Siemers KA, Nelson WJ
    Journal of cell science. 2002 ; 115 (Pt 8) : 1583-1590.
    PMID 11950877
    The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain.
    Berrueta L, Tirnauer JS, Schuyler SC, Pellman D, Bierer BE
    Current biology : CB. 1999 ; 9 (8) : 425-428.
    PMID 10226031
    Characterization of functional domains of human EB1 family proteins.
    Bu W, Su LK
    The Journal of biological chemistry. 2003 ; 278 (50) : 49721-49731.
    PMID 14514668
    CLIP-170 interacts with dynactin complex and the APC-binding protein EB1 by different mechanisms.
    Goodson HV, Skube SB, Stalder R, Valetti C, Kreis TE, Morrison EE, Schroer TA
    Cell motility and the cytoskeleton. 2003 ; 55 (3) : 156-173.
    PMID 12789661
    Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1).
    Hayashi I, Ikura M
    The Journal of biological chemistry. 2003 ; 278 (38) : 36430-36434.
    PMID 12857735
    Absence of somatic alterations of the EB1 gene adenomatous polyposis coli-associated protein in human sporadic colorectal cancers.
    Jaïs P, Sabourin JC, Bombled J, Rougier P, Lasser P, Duvillard P, Bénard J, Bressac-de Paillerets B
    British journal of cancer. 1998 ; 78 (10) : 1356-1360.
    PMID 9823979
    EB/RP gene family encodes tubulin binding proteins.
    Juwana JP, Henderikx P, Mischo A, Wadle A, Fadle N, Gerlach K, Arends JW, Hoogenboom H, Pfreundschuh M, Renner C
    International journal of cancer. Journal international du cancer. 1999 ; 81 (2) : 275-284.
    PMID 10188731
    Molecular linkage underlying microtubule orientation toward cortical sites in yeast.
    Korinek WS, Copeland MJ, Chaudhuri A, Chant J
    Science (New York, N.Y.). 2000 ; 287 (5461) : 2257-2259.
    PMID 10731146
    Positioning of the mitotic spindle by a cortical-microtubule capture mechanism.
    Lee L, Tirnauer JS, Li J, Schuyler SC, Liu JY, Pellman D
    Science (New York, N.Y.). 2000 ; 287 (5461) : 2260-2262.
    PMID 10731147
    The microtubule plus-end proteins EB1 and dynactin have differential effects on microtubule polymerization.
    Ligon LA, Shelly SS, Tokito M, Holzbaur EL
    Molecular biology of the cell. 2003 ; 14 (4) : 1405-1417.
    PMID 12686597
    Adenomatous polyposis coli and EB1 localize in close proximity of the mother centriole and EB1 is a functional component of centrosomes.
    Louie RK, Bahmanyar S, Siemers KA, Votin V, Chang P, Stearns T, Nelson WJ, Barth AI
    Journal of cell science. 2004 ; 117 (Pt 7) : 1117-1128.
    PMID 14970257
    A novel localization pattern for an EB1-like protein links microtubule dynamics to endomembrane organization.
    Mathur J, Mathur N, Kernebeck B, Srinivas BP, Hülskamp M
    Current biology : CB. 2003 ; 13 (22) : 1991-1997.
    PMID 14614826
    The dynamic behavior of the APC-binding protein EB1 on the distal ends of microtubules.
    Mimori-Kiyosue Y, Shiina N, Tsukita S
    Current biology : CB. 2000 ; 10 (14) : 865-868.
    PMID 10899006
    EB1, a protein which interacts with the APC tumour suppressor, is associated with the microtubule cytoskeleton throughout the cell cycle.
    Morrison EE, Wardleworth BN, Askham JM, Markham AF, Meredith DM
    Oncogene. 1998 ; 17 (26) : 3471-3477.
    PMID 10030671
    A cytokinesis checkpoint requiring the yeast homologue of an APC-binding protein.
    Muhua L, Adames NR, Murphy MD, Shields CR, Cooper JA
    Nature. 1998 ; 393 (6684) : 487-491.
    PMID 9624007
    Critical role for the EB1 and APC interaction in the regulation of microtubule polymerization.
    Nakamura M, Zhou XZ, Lu KP
    Current biology : CB. 2001 ; 11 (13) : 1062-1067.
    PMID 11470413
    RP1, a new member of the adenomatous polyposis coli-binding EB1-like gene family, is differentially expressed in activated T cells.
    Renner C, Pfitzenmeier JP, Gerlach K, Held G, Ohnesorge S, Sahin U, Bauer S, Pfreundschuh M
    Journal of immunology (Baltimore, Md. : 1950). 1997 ; 159 (3) : 1276-1283.
    PMID 9233623
    Drosophila EB1 is important for proper assembly, dynamics, and positioning of the mitotic spindle.
    Rogers SL, Rogers GC, Sharp DJ, Vale RD
    The Journal of cell biology. 2002 ; 158 (5) : 873-884.
    PMID 12213835
    Drosophila RhoGEF2 associates with microtubule plus ends in an EB1-dependent manner.
    Rogers SL, Wiedemann U, Häcker U, Turck C, Vale RD
    Current biology : CB. 2004 ; 14 (20) : 1827-1833.
    PMID 15498490
    BIM1 encodes a microtubule-binding protein in yeast.
    Schwartz K, Richards K, Botstein D
    Molecular biology of the cell. 1997 ; 8 (12) : 2677-2691.
    PMID 9398684
    APC binds to the novel protein EB1.
    Su LK, Burrell M, Hill DE, Gyuris J, Brent R, Wiltshire R, Trent J, Vogelstein B, Kinzler KW
    Cancer research. 1995 ; 55 (14) : 2972-2977.
    PMID 7606712
    Characterization of human MAPRE genes and their proteins.
    Su LK, Qi Y
    Genomics. 2001 ; 71 (2) : 142-149.
    PMID 11161807
    Shortstop recruits EB1/APC1 and promotes microtubule assembly at the muscle-tendon junction.
    Subramanian A, Prokop A, Yamamoto M, Sugimura K, Uemura T, Betschinger J, Knoblich JA, Volk T
    Current biology : CB. 2003 ; 13 (13) : 1086-1095.
    PMID 12842007
    EB1-microtubule interactions in Xenopus egg extracts: role of EB1 in microtubule stabilization and mechanisms of targeting to microtubules.
    Tirnauer JS, Grego S, Salmon ED, Mitchison TJ
    Molecular biology of the cell. 2002 ; 13 (10) : 3614-3626.
    PMID 12388761
    EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration.
    Wen Y, Eng CH, Schmoranzer J, Cabrera-Poch N, Morris EJ, Chen M, Wallar BJ, Alberts AS, Gundersen GG
    Nature cell biology. 2004 ; 6 (9) : 820-830.
    PMID 15311282


    This paper should be referenced as such :
    Tirnauer, JS
    MAPRE1 (Microtubule-associated protein, RP/EB family, member 1)
    Atlas Genet Cytogenet Oncol Haematol. 2005;9(1):3-5.
    Free journal version : [ pdf ]   [ DOI ]
    On line version :

    Other Leukemias implicated (Data extracted from papers in the Atlas) [ 3 ]
      t(11;20)(q23;q11) KMT2A/MAPRE1
    ins(9;4)(q33;q12q25) CDK5RAP2/PDGFRA
    t(11;20)(q23;q11) KMT2A/MAPRE1

    Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 1 ]
      MAPRE1/TM9SF4 (20q11)

    External links

    Genomic and cartography
    Gene and transcription
    RefSeq transcript (Entrez)
    RefSeq genomic (Entrez)
    SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
    BioGPS (Tissue expression)22919
    Protein : pattern, domain, 3D structure
    Domain families : Pfam (Sanger)
    Domain families : Pfam (NCBI)
    Protein Interaction databases
    Ontologies - Pathways
    Clinical trials, drugs, therapy
    canSAR (ICR) (select the gene name)
    REVIEW articlesautomatic search in PubMed
    Last year publicationsautomatic search in PubMed

    © Atlas of Genetics and Cytogenetics in Oncology and Haematology
    indexed on : Thu Oct 18 17:42:21 CEST 2018

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