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Gene Review

MAP2  -  microtubule-associated protein 2

Bos taurus

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Disease relevance of MAP2

  • The use of a panel of monoclonal antibodies (mAbs) directed against different determinants of microtubule-associated protein 2 (MAP2) enabled us to identify two distinct high-molecular-mass MAP2 species (270 and 250 kDa) and a substantial amount of MAP2c (70 kDa) in human neuroblastoma cells [1].
  • The stimulation by MAP2 occurred specifically in the activity of DNA polymerase alpha, but not DNA polymerases beta, gamma, and I from Escherichia coli [2].
  • By quantitative enzyme-linked immunosorbent assay (ELISA) a binding of single-shelled rotaviruses, which express vp6 on their surfaces, to purified MAP2 was found [3].
  • Pseudomonas spp. and Lactobacillus sakei were found in beef stored under MAP conditions with high oxygen content (MAP2), while Rahnella spp. and L. sakei were the main species found during storage using MAP3 [4].
  • One of the rotavirus cytosolic proteins, the inner capsid protein vp6, was expressed in axons at 48 hr p.i. simultaneously with the appearance of MAP2, while two other viral proteins, vp4 and NS28, remained in the nerve cell bodies [3].

Psychiatry related information on MAP2


High impact information on MAP2

  • Recent studies have shown that delayed neurotoxic organophosphorus compounds interact with Ca2+/calmodulin kinase II (CaM kinase II), an enzyme responsible for the endogenous phosphorylation of cytoskeletal proteins, i.e. microtubules, neurofilaments, and MAP-2 [6].
  • The filters were probed with purified bovine heart or brain RII, anti-RII monoclonal antibodies, and 125I-labeled protein A. Binding of RII was localized to a 31 amino acid sequence near the N-terminus of the MAP2 molecule [7].
  • MAP2 and tau exhibit microtubule-stabilizing activities that are implicated in the development and maintenance of neuronal axons and dendrites [8].
  • MAP2 binding and dissociation analyses revealed two affinity classes of binding sites on maize microtubules: a high-affinity site 12 dimers apart that may be homologous to the mammalian MAP2 binding site and an additional low-affinity site also 12 dimers apart that may be homologous to the mammalian tau binding site [9].
  • No cross-reaction with MAP 2, which is known to be extensively phosphorylated, other MAPs, or the low molecular weight neurofilament polypeptide was observed [10].

Biological context of MAP2

  • This state is perturbed by phosphorylation by MAP2 kinase, which affects all three activities by lowering the affinity of tau for the microtubule lattice [11].
  • Therefore, anchored PKA holoenzyme topology may position the catalytic subunit and MAP2 as to allow its preferential phosphorylation upon kinase activation [12].
  • There was a marked difference in the kinetics of tubulin polymerized in the presence of both taxol and MAP2 as compared to that obtained with either of them alone [13].
  • Disruption of RII alpha dimerization always prevented MAP2 interaction because 1) RII delta 1-14 (an amino-terminal deletion mutant lacking residues 1-14) was unable to bind MAP2 or form dimers, and 2) a modified RII alpha monomer including residues 1-14 did not bind MAP2 [12].
  • Here we examine the stabilizing effect of bovine brain MAP2 on microtubules assembled in interphase Xenopus egg extracts [14].

Anatomical context of MAP2


Associations of MAP2 with chemical compounds

  • Electron microscopy of thin sections of the MAP2-saturated microtubules fixed in the presence of tannic acid demonstrates a striking axial periodicity of 32 +/- 8 nm [15].
  • 1) Calmodulin affinity chromatography: both MAP2 and tau proteins were bound to calmodulin affinity columns in the presence of calcium and released with ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA), whereas tubulin was not bound [17].
  • 2) Cross-linking 125I-calmodulin to whole MAPs and MAP2 by disuccinimidyl suberate: 125I-calmodulin was cross-linked to MAP2 and tau proteins showing an intense radioactivity band at 300,000 daltons and a diffuse band between 70,000 and 90,000 daltons [17].
  • The results showed that the binding domain for MAP2 and P75 was located within the NH2-terminal 50 amino acids of RII beta [18].
  • MAP2 was modified selectively on its projection region by X-rhodamine iodoacetamide without altering the MT-binding activity [19].

Physical interactions of MAP2

  • These observations show that cdc2 kinase-dependent phosphorylation inhibits both the microtubule-stabilizing activity and the microtubule-nucleating activity of MAP2, while PKA-dependent phosphorylation affects only the microtubule-nucleating activity of MAP2 [20].
  • The MAP2 inhibition is reversed by a kinase that is co-purified with chicken embryonic MAP2, completely releasing MAP2 from the microtubules [21].
  • Polymers composed of normal alpha-tubulin and cleaved beta-tubulin or of cleaved alpha- and beta-tubulins were stabilized in the presence of added MAP2, myelin basic protein and histone H1 [22].

Enzymatic interactions of MAP2

  • In cdc2 kinase-phosphorylated MAP2, however, the phase transition from depolymerization to polymerization occurred with difficulty, with the result being that the half-life of individual microtubules was as short as in the absence of MAP2 [20].
  • The peptide map analysis revealed that calcineurin dephosphorylated MAP2 and tau factor universally, but not in a site-specific manner [23].

Regulatory relationships of MAP2


Other interactions of MAP2

  • Examination of spontaneous polymerization of microtubules using dark-field microscopy showed that the microtubule-nucleating activity of MAP2 was reduced by PKA-dependent phosphorylation and was completely abolished by cdc2 kinase-dependent phosphorylation [20].
  • Mapmodulin, a protein that interacts with the microtubule-associated proteins MAP2, MAP4, and tau, stimulates the microtubule- and dynein-dependent localization of Golgi complexes in semi-intact Chinese hamster ovary cells [25].
  • The results show that MAP1A microtubules were generally short and "straight' while those assembled with MAP1B were longer and "bendy'. MAP2 microtubules showed both types of morphologies even though straight microtubules were more abundant [26].
  • The concentrations of calmodulin required to give half-maximal activation of calcineurin were 21 and 16 nM with MAP2 and tau factor as substrates, respectively [23].
  • Thus, the phosphorylation of TH in bovine chromaffin cells appears to be regulated at three sites by three separate intracellular signaling pathways--Ser19 via Ca2+/calmodulin-dependent protein kinase II; Ser31 via ERK (MAP2 kinases); and Ser40 via cAMP-dependent protein kinase [27].

Analytical, diagnostic and therapeutic context of MAP2


  1. Characterization and intracellular distribution of microtubule-associated protein 2 in differentiating human neuroblastoma cells. Kirsch, J., Zutra, A., Littauer, U.Z. J. Neurochem. (1990) [Pubmed]
  2. Stimulation of DNA polymerase alpha activity by microtubule-associated proteins. Shioda, M., Okuhara, K., Murofushi, H., Mori, A., Sakai, H., Murakami-Murofushi, K., Suzuki, M., Yoshida, S. Biochemistry (1991) [Pubmed]
  3. Microtubule-associated protein 2 appears in axons of cultured dorsal root ganglia and spinal cord neurons after rotavirus infection. Weclewicz, K., Svensson, L., Billger, M., Holmberg, K., Wallin, M., Kristensson, K. J. Neurosci. Res. (1993) [Pubmed]
  4. Changes in the spoilage-related microbiota of beef during refrigerated storage under different packaging conditions. Ercolini, D., Russo, F., Torrieri, E., Masi, P., Villani, F. Appl. Environ. Microbiol. (2006) [Pubmed]
  5. Implication of brain cdc2 and MAP2 kinases in the phosphorylation of tau protein in Alzheimer's disease. Ledesma, M.D., Correas, I., Avila, J., Díaz-Nido, J. FEBS Lett. (1992) [Pubmed]
  6. Mechanisms of organophosphorus ester-induced delayed neurotoxicity: type I and type II. Abou-Donia, M.B., Lapadula, D.M. Annu. Rev. Pharmacol. Toxicol. (1990) [Pubmed]
  7. Localization and characterization of the binding site for the regulatory subunit of type II cAMP-dependent protein kinase on MAP2. Rubino, H.M., Dammerman, M., Shafit-Zagardo, B., Erlichman, J. Neuron (1989) [Pubmed]
  8. MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments. Al-Bassam, J., Ozer, R.S., Safer, D., Halpain, S., Milligan, R.A. J. Cell Biol. (2002) [Pubmed]
  9. Unique functional characteristics of the polymerization and MAP binding regulatory domains of plant tubulin. Hugdahl, J.D., Bokros, C.L., Hanesworth, V.R., Aalund, G.R., Morejohn, L.C. Plant Cell (1993) [Pubmed]
  10. A monoclonal antibody that cross-reacts with phosphorylated epitopes on two microtubule-associated proteins and two neurofilament polypeptides. Luca, F.C., Bloom, G.S., Vallee, R.B. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  11. Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Drechsel, D.N., Hyman, A.A., Cobb, M.H., Kirschner, M.W. Mol. Biol. Cell (1992) [Pubmed]
  12. Type II regulatory subunit dimerization determines the subcellular localization of the cAMP-dependent protein kinase. Scott, J.D., Stofko, R.E., McDonald, J.R., Comer, J.D., Vitalis, E.A., Mangili, J.A. J. Biol. Chem. (1990) [Pubmed]
  13. Taxol-induced polymerization of purified tubulin. Mechanism of action. Kumar, N. J. Biol. Chem. (1981) [Pubmed]
  14. cdc2 kinase-induced destabilization of MAP2-coated microtubules in Xenopus egg extracts. Faruki, S., Dorée, M., Karsenti, E. J. Cell. Sci. (1992) [Pubmed]
  15. The periodic association of MAP2 with brain microtubules in vitro. Kim, H., Binder, L.I., Rosenbaum, J.L. J. Cell Biol. (1979) [Pubmed]
  16. Microtubule-associated protein 2 (MAP2) is present in astrocytes of the optic nerve but absent from astrocytes of the optic tract. Papasozomenos, S.C., Binder, L.I. J. Neurosci. (1986) [Pubmed]
  17. Calmodulin binds to both microtubule-associated protein 2 and tau proteins. Lee, Y.C., Wolff, J. J. Biol. Chem. (1984) [Pubmed]
  18. Identification of the MAP2- and P75-binding domain in the regulatory subunit (RII beta) of type II cAMP-dependent protein kinase. Cloning and expression of the cDNA for bovine brain RII beta. Luo, Z., Shafit-Zagardo, B., Erlichman, J. J. Biol. Chem. (1990) [Pubmed]
  19. Visualization of the stop of microtubule depolymerization that occurs at the high-density region of microtubule-associated protein 2 (MAP2). Ichihara, K., Kitazawa, H., Iguchi, Y., Hotani, H., Itoh, T.J. J. Mol. Biol. (2001) [Pubmed]
  20. Phosphorylation states of microtubule-associated protein 2 (MAP2) determine the regulatory role of MAP2 in microtubule dynamics. Itoh, T.J., Hisanaga, S., Hosoi, T., Kishimoto, T., Hotani, H. Biochemistry (1997) [Pubmed]
  21. A microtubule-associated protein (MAP2) kinase restores microtubule motility in embryonic brain. López, L.A., Sheetz, M.P. J. Biol. Chem. (1995) [Pubmed]
  22. Stabilization and bundling of subtilisin-treated microtubules induced by microtubule associated proteins. Saoudi, Y., Paintrand, I., Multigner, L., Job, D. J. Cell. Sci. (1995) [Pubmed]
  23. Dephosphorylation of microtubule-associated protein 2, tau factor, and tubulin by calcineurin. Goto, S., Yamamoto, H., Fukunaga, K., Iwasa, T., Matsukado, Y., Miyamoto, E. J. Neurochem. (1985) [Pubmed]
  24. Activation of a microtubule-associated protein-2 kinase by insulin-like growth factor-I in bovine chromaffin cells. Cahill, A.L., Perlman, R.L. J. Neurochem. (1991) [Pubmed]
  25. Mapmodulin, cytoplasmic dynein, and microtubules enhance the transport of mannose 6-phosphate receptors from endosomes to the trans-golgi network. Itin, C., Ulitzur, N., Mühlbauer, B., Pfeffer, S.R. Mol. Biol. Cell (1999) [Pubmed]
  26. Modulation of microtubule shape in vitro by high molecular weight microtubule associated proteins MAP1A, MAP1B, and MAP2. Pedrotti, B., Francolini, M., Cotelli, F., Islam, K. FEBS Lett. (1996) [Pubmed]
  27. Multiple signaling pathways in bovine chromaffin cells regulate tyrosine hydroxylase phosphorylation at Ser19, Ser31, and Ser40. Haycock, J.W. Neurochem. Res. (1993) [Pubmed]
  28. Exploring the microtubule-binding region of bovine microtubule-associated protein-2 (MAP-2): cDNA sequencing, bacterial expression, and site-directed mutagenesis. Coffey, R.L., Joly, J.C., Cain, B.D., Purich, D.L. Biochemistry (1994) [Pubmed]
  29. Interactions of microtubule-associated protein MAP2 with unpolymerized and polymerized tubulin and actin using a 96-well microtiter plate solid-phase immunoassay. Pedrotti, B., Colombo, R., Islam, K. Biochemistry (1994) [Pubmed]
  30. Ca2+, calmodulin-dependent regulation of microtubule formation via phosphorylation of microtubule-associated protein 2, tau factor, and tubulin, and comparison with the cyclic AMP-dependent phosphorylation. Yamamoto, H., Fukunaga, K., Goto, S., Tanaka, E., Miyamoto, E. J. Neurochem. (1985) [Pubmed]
  31. MAP2 competes with MAP1 for binding to microtubules. Kuznetsov, S.A., Rodionov, V.I., Gelfand, V.I., Rosenblat, V.A. Biochem. Biophys. Res. Commun. (1984) [Pubmed]
  32. Mapping of distinct structural domains on microtubule-associated protein 2 by monoclonal antibodies. Scherson, T., Geiger, B., Eshhar, Z., Littauer, U.Z. Eur. J. Biochem. (1982) [Pubmed]
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