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Gene Review

MOAP1  -  modulator of apoptosis 1

Homo sapiens

Synonyms: MAP-1, MAP1, Modulator of apoptosis 1, PNMA4, Paraneoplastic antigen Ma4
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Disease relevance of MOAP1

  • Similarly, homologues of MAP-1 in other phylogenetically and antigenically related ehrlichial agents such as Anaplasma marginale and Ehrlichia chaffeensis are also targets of protective responses [1].
  • Expression of microtubule-associated proteins, MAP-1 and MAP-2, in human neuroblastomas and differential diagnosis of immature neuroblasts [2].
  • Other types of round-cell tumors examined, including several cases of Ewing's sarcoma, undifferentiated rhabdomyosarcoma, and malignant lymphoma, showed no reaction with antibodies to MAP-1 and MAP-2 [2].
  • The map1 gene of Cowdria ruminantium is a member of a multigene family containing both conserved and variable genes [3].
  • The fact that aromatic amino acids have been found to be the most representative of A-signal [Kuspa, A., Plamann, L. & Kaiser, D. (1992) J. Bacteriol. 174, 3319-3326] is consistent with the hypothesis that, regarding its specificity, MAP1 is likely to play a role in development of myxobacteria [4].

Psychiatry related information on MOAP1

  • However, the amount of tau protein or MAP1 from the brains of Alzheimer's disease patients was about half of that present in their control counterparts [5].
  • The hyperphosphorylated tau sequesters normal tau, MAP1 and MAP2, which results in breakdown of the microtubule network and, consequently, a progressive retrograde degeneration of the affected neurons and, ultimately, dementia [6].

High impact information on MOAP1

  • RASSF1A/MAP-1 binding relieved this inhibitory interaction, resulting in MAP-1 association with Bax [7].
  • The tumor suppressor RASSF1A and MAP-1 link death receptor signaling to Bax conformational change and cell death [7].
  • Taken together the data suggested that estramustine binds to a 330-kD MAP-1-like protein to disrupt microtubules in tumor cells [8].
  • Estramustine binds a MAP-1-like protein to inhibit microtubule assembly in vitro and disrupt microtubule organization in DU 145 cells [8].
  • These surprising results contrast sharply with reported dramatic developmental increases in the amount of MAP1 in brain and in nerve growth factor-induced PC12 cells [9].

Chemical compound and disease context of MOAP1

  • A DNA vaccine (VCL1010/MAP1) containing the major antigenic protein 1 (MAP1) gene of Cowdria ruminantium, driven by the human cytomegalovirus (HCMV) enhancer-promoter, was injected intramuscularly into 8-10 week-old female DBA/2 mice after treating them with 50 microliters/muscle of 0.5% bupivacaine three days previously [10].
  • METHODS: Patients with refractory or recurrent acute lymphoblastic leukemia (ALL) were treated with a combination of methotrexate (MTX), vincristine, PEG-asparaginase, and prednisone (MOAP) [11].

Biological context of MOAP1

  • We now identify a novel pathway connecting RASSF1A to Bax via the Bax binding protein MOAP-1 [12].
  • A 280-kDa protein (p280) confined to the nucleus of interphase cells becomes associated with the mitotic spindle during cell division. p280 is immunologically related to the microtubule-associated protein MAP1, as shown by cross-reactivity with monoclonal (8D12) and polyclonal antibodies raised against MAP1 [13].
  • Results of yeast two-hybrid analysis suggested that Map1 may physically interact with Mat1-Pc, the product of the h(+)-specific mating-type gene mat1-Pc [14].
  • PolyQ72, but not polyQ11, stimulated Atg5-Atg12-Atg16 complex-dependent microtubule-associated protein 1 (MAP1) light chain 3 (LC3) conversion from LC3-I to -II, which plays a key role in autophagy [15].
  • We have examined the post-translational modification of high molecular weight microtubule-associated proteins (MAPs) have shown that MAP1, MAP2, and MAP4 are glycosylated [16].

Anatomical context of MOAP1

  • As one of the downstream modulaters of GR activation, Bax can be up regulated and translocated to the mitochondria, where it binds to modulator of apoptosis-1 (MAP-1), a mitochondrial effector of BAX to cause change Deltapsi [17].
  • The MAP1-specific cDNA probes were used in blot transfer experiments with RNA prepared from brain, liver, kidney, stomach, spleen, and thymus [9].
  • The occurrence and cellular localization of polypeptides related to hog brain microtubule-associated proteins 1 and 2 (MAP-1 and MAP-2) in non-neuronal cell lines of various species and types, and in several tissues from rat was studied [18].
  • Immunoblotting of preparations from 3T6, CHO, HeLa and N2A cells, as well as pituitary, heart, testis and liver revealed immuno-reactivity with antibodies to neuronal MAP-1 for polypeptides co-migrating with MAP-1 in all cases, except for HeLa cells and liver [18].
  • As shown by double immunofluorescence microscopy of various cultured cell lines using affinity-purified antibodies to MAPs, and monoclonal antibodies to tubulin, MAP-1-as well as MAP-2-related antigens were generally, but not exclusively, associated with typical microtubule structures of the cytoplasm, spindle, midbody and primary cilia [18].

Associations of MOAP1 with chemical compounds

  • The MAP 1 minute and 10 minutes after ECT (101.25 [7.5] mm Hg and 100.16 [11.0] mm Hg, respectively) was significantly increased compared with before ECT (94.56 [6.9] mm Hg) in sevoflurane group (P < 0.05) [19].
  • Three different conditions for preserving fresh sausages were tested: MAP1 (20% CO2, 70% O2, and 10% N2), MAP2 (40% CO2 and 60% O2), and MAP3 (40% CO2, 30% O2, and 30% N2) [20].

Regulatory relationships of MOAP1


Other interactions of MOAP1

  • Our findings identify RASSF1A and MAP-1 as important components between death receptors and the apoptotic machinery and reveal a potential link between tumor suppression and death receptor signaling [7].
  • Late in infection (24-36 h) the anti-apoptotic genes largely shut down and the pro-apoptotic genes, including Nip3, Hrk, Bak, Bik, Bok, Bax, Bad, Bim and Moap-1, were activated [21].

Analytical, diagnostic and therapeutic context of MOAP1

  • Genetic immunizations with the gene encoding MAP-1 induce protective T helper cell type 1 responses against lethal challenge in a mouse model [1].
  • Immunocytochemistry shows that after 3 days in culture with CT beta, DEV cells develop processes which stain positive for neurofilaments and MAP-1 [22].
  • We demonstrate, by sequence analysis, that map1 encoding the major outer membrane protein of C. ruminantium is also encoded by a polymorphic multigene family [3].
  • An extracellular elastase, termed Myxococcus xanthus alkaline protease 1 (MAP1), has been purified from M. xanthus DK1622 culture supernatants by a combination of ion-exchange and affinity chromatographies [4].
  • Two major antigenic proteins (MAPs), MAP1 and MAP2, have been examined for their use as antigens in the serodiagnosis of heartwater [23].


  1. Vaccine strategies for Cowdria ruminantium infections and their application to other ehrlichial infections. Mahan, S.M., Allsopp, B., Kocan, K.M., Palmer, G.H., Jongejan, F. Parasitol. Today (Regul. Ed.) (1999) [Pubmed]
  2. Expression of microtubule-associated proteins, MAP-1 and MAP-2, in human neuroblastomas and differential diagnosis of immature neuroblasts. Artlieb, U., Krepler, R., Wiche, G. Lab. Invest. (1985) [Pubmed]
  3. The map1 gene of Cowdria ruminantium is a member of a multigene family containing both conserved and variable genes. Sulsona, C.R., Mahan, S.M., Barbet, A.F. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  4. Purification and characterization of an alkaline elastase from Myxococcus xanthus. Dumont, L., Verneuil, B., Wallach, J., Julien, R. Eur. J. Biochem. (1994) [Pubmed]
  5. Altered levels of microtubule proteins in brains of Alzheimer's disease patients. Nieto, A., Montejo de Garcini, E., Avila, J. Acta Neuropathol. (1989) [Pubmed]
  6. Metabolic/signal transduction hypothesis of Alzheimer's disease and other tauopathies. Iqbal, K., Grundke-Iqbal, I. Acta Neuropathol. (2005) [Pubmed]
  7. The tumor suppressor RASSF1A and MAP-1 link death receptor signaling to Bax conformational change and cell death. Baksh, S., Tommasi, S., Fenton, S., Yu, V.C., Martins, L.M., Pfeifer, G.P., Latif, F., Downward, J., Neel, B.G. Mol. Cell (2005) [Pubmed]
  8. Estramustine binds a MAP-1-like protein to inhibit microtubule assembly in vitro and disrupt microtubule organization in DU 145 cells. Stearns, M.E., Wang, M., Tew, K.D., Binder, L.I. J. Cell Biol. (1988) [Pubmed]
  9. A cloned cDNA encoding MAP1 detects a single copy gene in mouse and a brain-abundant RNA whose level decreases during development. Lewis, S.A., Sherline, P., Cowan, N.J. J. Cell Biol. (1986) [Pubmed]
  10. A DNA vaccine protects mice against the rickettsial agent Cowdria ruminantium. Nyika, A., Mahan, S.M., Burridge, M.J., Mcguire, T.C., Rurangirwa, F., Barbet, A.F. Parasite Immunol. (1998) [Pubmed]
  11. Combination therapy with methotrexate, vincristine, polyethylene-glycol conjugated-asparaginase, and prednisone in the treatment of patients with refractory or recurrent acute lymphoblastic leukemia. Aguayo, A., Cortes, J., Thomas, D., Pierce, S., Keating, M., Kantarjian, H. Cancer (1999) [Pubmed]
  12. The RASSF1A tumor suppressor activates Bax via MOAP-1. Vos, M.D., Dallol, A., Eckfeld, K., Allen, N.P., Donninger, H., Hesson, L.B., Calvisi, D., Latif, F., Clark, G.J. J. Biol. Chem. (2006) [Pubmed]
  13. A widely distributed nuclear protein immunologically related to the microtubule-associated protein MAP1 is associated with the mitotic spindle. Bonifacino, J.S., Klausner, R.D., Sandoval, I.V. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  14. Schizosaccharomyces pombe map1+ encodes a MADS-box-family protein required for cell-type-specific gene expression. Yabana, N., Yamamoto, M. Mol. Cell. Biol. (1996) [Pubmed]
  15. ER stress (PERK/eIF2alpha phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation. Kouroku, Y., Fujita, E., Tanida, I., Ueno, T., Isoai, A., Kumagai, H., Ogawa, S., Kaufman, R.J., Kominami, E., Momoi, T. Cell Death Differ. (2007) [Pubmed]
  16. High molecular weight microtubule-associated proteins contain O-linked-N-acetylglucosamine. Ding, M., Vandré, D.D. J. Biol. Chem. (1996) [Pubmed]
  17. Stress-induced change of mitochondria membrane potential regulated by genomic and non-genomic GR signaling: A possible mechanism for hippocampus atrophy in PTSD. Zhang, L., Zhou, R., Li, X., Ursano, R.J., Li, H. Med. Hypotheses (2006) [Pubmed]
  18. Widespread occurrence of polypeptides related to neurotubule-associated proteins (MAP-1 and MAP-2) in non-neuronal cells and tissues. Wiche, G., Briones, E., Koszka, C., Artlieb, U., Krepler, R. EMBO J. (1984) [Pubmed]
  19. Sevoflurane as an alternative anaesthetic for electroconvulsive therapy. Toprak, H.I., Gedik, E., Begeç, Z., Oztürk, E., Kaya, B., Ersoy, M.O. The journal of ECT. (2005) [Pubmed]
  20. Shelf life of fresh sausages stored under modified atmospheres. Tremonte, P., Sorrentino, E., Succi, M., Reale, A., Maiorano, G., Coppola, R. J. Food Prot. (2005) [Pubmed]
  21. Temporal activation of anti- and pro-apoptotic factors in human gingival fibroblasts infected with the periodontal pathogen, Porphyromonas gingivalis: potential role of bacterial proteases in host signalling. Urnowey, S., Ansai, T., Bitko, V., Nakayama, K., Takehara, T., Barik, S. BMC Microbiol. (2006) [Pubmed]
  22. Cholera toxin beta subunit induces the differentiation of human medulloblastoma cell line DEV in a neuronal pathway. Dufay, N., Belin, M.F., Confavreux, C., Touraine-Moulin, F., Derrington, E.A. Eur. J. Neurosci. (1994) [Pubmed]
  23. Potential value of major antigenic protein 2 for serological diagnosis of heartwater and related ehrlichial infections. Bowie, M.V., Reddy, G.R., Semu, S.M., Mahan, S.M., Barbet, A.F. Clin. Diagn. Lab. Immunol. (1999) [Pubmed]
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