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Gene Review

MAP1B  -  microtubule-associated protein 1B

Homo sapiens

Synonyms: FUTSCH, MAP-1B, MAP5, Microtubule-associated protein 1B, PPP1R102
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Disease relevance of MAP1B


Psychiatry related information on MAP1B


High impact information on MAP1B

  • The protein MAP-1B links GABA(C) receptors to the cytoskeleton at retinal synapses [7].
  • Furthermore, GABA(C) receptors and MAP-1B co-localize at postsynaptic sites on bipolar cell axon terminals [7].
  • Recognized now as one of the most abundant axonal microtubule-associated proteins, a convergence of evidence implicates an overlapping in vivo role of tau with other axonal microtubule-associated proteins (e.g. MAP1B) in establishing microtubule stability, axon elongation and axonal structure [8].
  • The interaction of MAG with MAP1B is relevant to the known role of MAG in affecting the cytoskeletal structure and stability of myelinated axons [9].
  • In addition, expression of the phosphorylated isoform of MAP1B was increased significantly when DRGNs were cocultured with MAG-transfected COS cells [9].

Chemical compound and disease context of MAP1B


Biological context of MAP1B

  • Binding sites for a MAG-Fc chimera on DRGNs colocalized with MAP1B on neuronal varicosities, and MAG and MAP1B also colocalized in the periaxonal region of myelinated axons [9].
  • The gene includes seven exons, and the third exon contains sequence not represented in mouse or rat MAP1B [11].
  • The exon/intron organization underlying the alternative transcripts and the N-terminal amino acid sequence of the putative truncated MAP1B isoforms resemble those of MAP1A, providing further evidence for an evolutionary relationship [12].
  • Moreover, we show that overexpression of MAP1B in wild-type cortical neurons leads to cell death characteristic of GAN-null neurons, whereas reducing MAP1B levels significantly improves the survival rate of null neurons [13].
  • Mammalian genomes usually contain three family members, MAP1A, MAP1B and a shorter, more recently identified gene called MAP1S [14].

Anatomical context of MAP1B

  • The expression of some MAP1B as a neuronal plasma membrane glycoprotein (Tanner, S.L., R. Franzen, H. Jaffe, and R.H. Quarles. 2000. J. Neurochem. 75:553-562.), further documented here by its immunostaining without cell permeabilization, is consistent with it being a binding partner for MAG on the axonal surface [9].
  • C19ORF5 is a sequence homologue of microtubule-associated proteins MAP1A/MAP1B of unknown function, except for its association with mitochondria-associated proteins and the paclitaxel-like microtubule stabilizer and candidate tumor suppressor RASSF1A [15].
  • MAP2 and MAP1B also accumulated in neuronal cell bodies prior to a loss of immunostaining in some regions, notably subiculum [1].
  • Microtubule-associated proteins 1A (MAP1A) and MAP1B are abundant neuronal MAPs thought to be involved in neurite formation and stabilization [16].
  • Contact with astroglial membranes induces axonal and dendritic growth of human CNS model neurons and affects the distribution of the growth-associated proteins MAP1B and GAP43 [17].

Associations of MAP1B with chemical compounds

  • Consistently with this hypothesis, a major pool of MAP1B HC is rapidly degraded after blocking protein synthesis with cycloheximide, whereas LC1 levels remain constant even after 24 hr of cycloheximide treatment [18].
  • Furthermore, the endogenous degradation of MAPs in neonate brain homogenates was calcium-dependent and inhibited by leupeptin, and the pattern of degradation products for MAP1B and MAP2 was similar to that of calpain-mediated proteolysis [19].
  • Distinct from all other MAPs, the MAP1B light chain-induced formation of stable but apparently flexible microtubules resistant to the effects of nocodazole and taxol [20].
  • Betamethasone exposure resulted in decreased immunoreactivity (IR) of MAP1B by 34.3 % and MAP2abc by 34.1 % (P < 0.05) [21].
  • Furthermore, MAP1B in intact DRGNs is readily degraded by extracellular trypsin and is labeled by the cell surface probe sulfosuccinimidobiotin [3].

Physical interactions of MAP1B

  • C19ORF5 is a homologue of microtubule-associated protein MAP1B that interacts with natural paclitaxel-like microtubule stabilizer and candidate tumor suppressor RASSF1A [22].
  • MAP-1B also bound in vitro assembled alpha-synuclein fibrils [23].
  • Diminished protein levels of the microtubule-associated protein MAP1B and increased levels of the GTP-binding protein RND2 were confirmed in the developing cortex in vivo and in primary hippocampal neurons in vitro [24].
  • In addition, we found posttranscriptional regulation of MAP1B mRNA by the selective RNA-binding protein QKI in oligodendroglia [25].
  • This suggests that SCG10 is more potent to destabilize microtubules than MAP1B to rescue them [26].

Regulatory relationships of MAP1B

  • Furthermore, forced expression of exogenous QKI was sufficient for promoting MAP1B expression [25].

Other interactions of MAP1B


Analytical, diagnostic and therapeutic context of MAP1B

  • MAP1B heavy chain (HC) and light chain (LC1), as well as the light chain of MAP1A (LC2), were prepared in purified form for use as standards and/or immunogens for generation of antibodies for immunoblotting [18].
  • In situ hybridization with MAP1B antisense riboprobe showed markedly increased hybridization signal intensities in the large neurons, whereas neurons in the normal-appearing cortex and most of the normal-sized neurons in the dysplastic cortex had faint signals [30].
  • By immunoelectron microscopy, the products of the reaction with the anti-S 100 antibody appeared as heterogeneous granular deposits and with the antibody to MAP 1B they were randomly scattered throughout the astrocytic inclusions [31].
  • Here we have analyzed the effects of the MAP1B light chain in the absence or presence of the heavy chain by immunofluorescence microscopy of transiently transfected cells [20].
  • Confirmation of induced expression of MAP1B mRNA was obtained by PCR with specific primers and by immunocytochemical analysis in cultured RPE cells and in surgically removed epiretinal membranes from patients with proliferative vitreoretinopathy [32].


  1. Postmortem changes in the levels and localization of microtubule-associated proteins (tau, MAP2 and MAP1B) in the rat and human hippocampus. Schwab, C., Bondada, V., Sparks, D.L., Cahan, L.D., Geddes, J.W. Hippocampus. (1994) [Pubmed]
  2. Upregulation of MAP1B and MAP2 in the rat brain after middle cerebral artery occlusion: effect of age. Popa-Wagner, A., Schröder, E., Schmoll, H., Walker, L.C., Kessler, C. J. Cereb. Blood Flow Metab. (1999) [Pubmed]
  3. Evidence for expression of some microtubule-associated protein 1B in neurons as a plasma membrane glycoprotein. Tanner, S.L., Franzen, R., Jaffe, H., Quarles, R.H. J. Neurochem. (2000) [Pubmed]
  4. Mapping of human microtubule-associated protein 1B in proximity to the spinal muscular atrophy locus at 5q13. Lien, L.L., Boyce, F.M., Kleyn, P., Brzustowicz, L.M., Menninger, J., Ward, D.C., Gilliam, T.C., Kunkel, L.M. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  5. Immunohistochemical expression of microtubule-associated protein 5 (MAP5) in glial cells in multiple system atrophy. Arai, N., Nishimura, M., Oda, M., Morimatsu, Y., Ohe, R., Nagatomo, H. J. Neurol. Sci. (1992) [Pubmed]
  6. Immunochemical evidence that fragments of phosphorylated MAP5 (MAP1B) are bound to neurofibrillary tangles in Alzheimer's disease. Hasegawa, M., Arai, T., Ihara, Y. Neuron (1990) [Pubmed]
  7. The protein MAP-1B links GABA(C) receptors to the cytoskeleton at retinal synapses. Hanley, J.G., Koulen, P., Bedford, F., Gordon-Weeks, P.R., Moss, S.J. Nature (1999) [Pubmed]
  8. Going new places using an old MAP: tau, microtubules and human neurodegenerative disease. Garcia, M.L., Cleveland, D.W. Curr. Opin. Cell Biol. (2001) [Pubmed]
  9. Microtubule-associated protein 1B: a neuronal binding partner for myelin-associated glycoprotein. Franzen, R., Tanner, S.L., Dashiell, S.M., Rottkamp, C.A., Hammer, J.A., Quarles, R.H. J. Cell Biol. (2001) [Pubmed]
  10. Implication of cyclin-dependent kinases and glycogen synthase kinase 3 in the phosphorylation of microtubule-associated protein 1B in developing neuronal cells. García-Pérez, J., Avila, J., Díaz-Nido, J. J. Neurosci. Res. (1998) [Pubmed]
  11. Cloning of human microtubule-associated protein 1B and the identification of a related gene on chromosome 15. Lien, L.L., Feener, C.A., Fischbach, N., Kunkel, L.M. Genomics (1994) [Pubmed]
  12. The mouse and rat MAP1B genes: genomic organization and alternative transcription. Kutschera, W., Zauner, W., Wiche, G., Propst, F. Genomics (1998) [Pubmed]
  13. Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival. Allen, E., Ding, J., Wang, W., Pramanik, S., Chou, J., Yau, V., Yang, Y. Nature (2005) [Pubmed]
  14. The MAP1 family of microtubule-associated proteins. Halpain, S., Dehmelt, L. Genome Biol. (2006) [Pubmed]
  15. Distinct structural domains within C19ORF5 support association with stabilized microtubules and mitochondrial aggregation and genome destruction. Liu, L., Vo, A., Liu, G., McKeehan, W.L. Cancer Res. (2005) [Pubmed]
  16. Gene localization and developmental expression of light chain 3: a common subunit of microtubule-associated protein 1A(MAP1A) and MAP1B. Mann, S.S., Hammarback, J.A. J. Neurosci. Res. (1996) [Pubmed]
  17. Contact with astroglial membranes induces axonal and dendritic growth of human CNS model neurons and affects the distribution of the growth-associated proteins MAP1B and GAP43. Piontek, J., Régnier-Vigouroux, A., Brandt, R. J. Neurosci. Res. (2002) [Pubmed]
  18. Regulation of microtubule-associated protein 1B (MAP1B) subunit composition. Mei, X., Sweatt, A.J., Hammarback, J.A. J. Neurosci. Res. (2000) [Pubmed]
  19. Calpain-mediated proteolysis of microtubule associated proteins MAP1B and MAP2 in developing brain. Fischer, I., Romano-Clarke, G., Grynspan, F. Neurochem. Res. (1991) [Pubmed]
  20. Novel features of the light chain of microtubule-associated protein MAP1B: microtubule stabilization, self interaction, actin filament binding, and regulation by the heavy chain. Tögel, M., Wiche, G., Propst, F. J. Cell Biol. (1998) [Pubmed]
  21. Glucocorticoid exposure at the dose used clinically alters cytoskeletal proteins and presynaptic terminals in the fetal baboon brain. Antonow-Schlorke, I., Schwab, M., Li, C., Nathanielsz, P.W. J. Physiol. (Lond.) (2003) [Pubmed]
  22. Putative tumor suppressor RASSF1 interactive protein and cell death inducer C19ORF5 is a DNA binding protein. Liu, L., Vo, A., Liu, G., McKeehan, W.L. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  23. Microtubule-associated protein 1B is a component of cortical Lewy bodies and binds alpha-synuclein filaments. Jensen, P.H., Islam, K., Kenney, J., Nielsen, M.S., Power, J., Gai, W.P. J. Biol. Chem. (2000) [Pubmed]
  24. COUP-TFI is required for the formation of commissural projections in the forebrain by regulating axonal growth. Armentano, M., Filosa, A., Andolfi, G., Studer, M. Development (2006) [Pubmed]
  25. QKI Binds MAP1B mRNA and Enhances MAP1B Expression during Oligodendrocyte Development. Zhao, L., Ku, L., Chen, Y., Xia, M., Lopresti, P., Feng, Y. Mol. Biol. Cell (2006) [Pubmed]
  26. The control of microtubule stability in vitro and in transfected cells by MAP1B and SCG10. Bondallaz, P., Barbier, A., Soehrman, S., Grenningloh, G., Riederer, B.M. Cell Motil. Cytoskeleton (2006) [Pubmed]
  27. Identification and characterization of human VCY2-interacting protein: VCY2IP-1, a microtubule-associated protein-like protein. Wong, E.Y., Tse, J.Y., Yao, K.M., Lui, V.C., Tam, P.C., Yeung, W.S. Biol. Reprod. (2004) [Pubmed]
  28. Intermediate filament aggregation in fibroblasts of giant axonal neuropathy patients is aggravated in non dividing cells and by microtubule destabilization. Bomont, P., Koenig, M. Hum. Mol. Genet. (2003) [Pubmed]
  29. A role for semaphorin 3A signaling in the degeneration of hippocampal neurons during Alzheimer's disease. Good, P.F., Alapat, D., Hsu, A., Chu, C., Perl, D., Wen, X., Burstein, D.E., Kohtz, D.S. J. Neurochem. (2004) [Pubmed]
  30. Early forms of microtubule-associated protein are strongly expressed in cortical dysplasia. Yamanouchi, H., Jay, V., Otsubo, H., Kaga, M., Becker, L.E., Takashima, S. Acta Neuropathol. (1998) [Pubmed]
  31. Immunohistochemical studies on the new type of astrocytic inclusions identified in a patient with brain malformation. Kato, S., Hirano, A., Umahara, T., Herz, F., Shioda, K., Minagawa, M. Acta Neuropathol. (1992) [Pubmed]
  32. Expression and upregulation of microtubule-associated protein 1B in cultured retinal pigment epithelial cells. Esser, P., Grisanti, S., Kociok, N., Abts, H., Hueber, A., Unfried, K., Heimann, K., Weller, M. Invest. Ophthalmol. Vis. Sci. (1997) [Pubmed]
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