微小管結合タンパク質2
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- microtubule-associated protein 2
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2018/04/13 03:09:52」(JST)
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MAP2 |
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Identifiers |
Aliases |
MAP2, MAP2A, MAP2B, MAP2C, microtubule associated protein 2 |
External IDs |
MGI: 97175 HomoloGene: 1779 GeneCards: MAP2 |
Gene location (Human) |
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Chr. |
Chromosome 2 (human)[1] |
|
Band |
2q34 |
Start |
209,424,058 bp[1] |
End |
209,734,118 bp[1] |
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Gene location (Mouse) |
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Chr. |
Chromosome 1 (mouse)[2] |
|
Band |
1 C3|1 33.49 cM |
Start |
66,175,273 bp[2] |
End |
66,442,583 bp[2] |
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RNA expression pattern |
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More reference expression data |
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Gene ontology |
Molecular function |
• tubulin binding
• protein binding
• structural molecule activity
• dystroglycan binding
• calmodulin binding
• microtubule binding
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Cellular component |
• nucleolus
• microtubule
• microtubule associated complex
• cytoskeleton
• cytoplasm
• cytosol
• dendrite
• cell projection
• intracellular
• postsynaptic density
• nuclear periphery
• neuron projection
• neuronal cell body
• dendritic shaft
• cell body
• CA3 pyramidal cell dendrite
|
Biological process |
• neuron projection development
• microtubule cytoskeleton organization
• microtubule bundle formation
• dendrite morphogenesis
• central nervous system neuron development
• axonogenesis
• dendrite development
• establishment of cell polarity
• regulation of axonogenesis
• cellular response to organic substance
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Sources:Amigo / QuickGO |
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Orthologs |
Species |
Human |
Mouse |
Entrez |
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Ensembl |
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UniProt |
|
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RefSeq (mRNA) |
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NM_001039538
NM_002374
NM_031845
NM_031846
NM_031847
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|
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NM_001039934
NM_008632
NM_001310634
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RefSeq (protein) |
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NP_001034627
NP_002365
NP_114033
NP_114035
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NP_001035023
NP_001297563
NP_032658
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Location (UCSC) |
Chr 2: 209.42 – 209.73 Mb |
Chr 1: 66.18 – 66.44 Mb |
PubMed search |
[3] |
[4] |
Wikidata |
View/Edit Human |
View/Edit Mouse |
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Microtubule-associated protein 2 is a protein that in humans is encoded by the MAP2 gene.[5][6]
Contents
- 1 Function
- 2 Interactions
- 3 References
- 4 Further reading
Function
This gene encodes a protein that belongs to the microtubule-associated protein family. The proteins of this family are thought to be involved in microtubule assembly, which is an essential step in neuritogenesis. MAP2 serves to stabilize microtubules (MT) growth by crosslinking MT with intermediate filaments and other MTs. The products of similar genes in rat and mouse are neuron-specific cytoskeletal proteins that are enriched in dendrites, implicating a role in determining and stabilizing dendritic shape during neuron development. A number of alternatively spliced variants encoding distinct isoforms have been described.[7]
Interactions
MAP2 has been shown to interact with Grb2,[8][9] NEFL[10] and MYO7A.[11] MAP2 is suspected of interacting with tubulin.
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000078018 - Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000015222 - Ensembl, May 2017
- ^ "Human PubMed Reference:".
- ^ "Mouse PubMed Reference:".
- ^ Neve RL, Harris P, Kosik KS, Kurnit DM, Donlon TA (May 1987). "Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2". Brain Res. 387 (3): 271–80. PMID 3103857.
- ^ Kalcheva N, Albala J, O'Guin K, Rubino H, Garner C, Shafit-Zagardo B (December 1995). "Genomic structure of human microtubule-associated protein 2 (MAP-2) and characterization of additional MAP-2 isoforms". Proc Natl Acad Sci U S A. 92 (24): 10894–8. doi:10.1073/pnas.92.24.10894. PMC 40537 . PMID 7479905.
- ^ "Entrez Gene: MAP2 microtubule-associated protein 2".
- ^ Lim RW, Halpain S (July 2000). "Regulated association of microtubule-associated protein 2 (MAP2) with Src and Grb2: evidence for MAP2 as a scaffolding protein". J. Biol. Chem. 275 (27): 20578–87. doi:10.1074/jbc.M001887200. PMID 10781592.
- ^ Zamora-Leon SP, Lee G, Davies P, Shafit-Zagardo B (October 2001). "Binding of Fyn to MAP-2c through an SH3 binding domain. Regulation of the interaction by ERK2". J. Biol. Chem. 276 (43): 39950–8. doi:10.1074/jbc.M107807200. PMID 11546790.
- ^ Frappier T, Stetzkowski-Marden F, Pradel LA (April 1991). "Interaction domains of neurofilament light chain and brain spectrin". Biochem. J. 275 (Pt 2): 521–7. doi:10.1042/bj2750521. PMC 1150082 . PMID 1902666.
- ^ Todorov PT, Hardisty RE, Brown SD (March 2001). "Myosin VIIA is specifically associated with calmodulin and microtubule-associated protein-2B (MAP-2B)". Biochem. J. 354 (Pt 2): 267–74. doi:10.1042/0264-6021:3540267. PMC 1221652 . PMID 11171103.
Further reading
- Roses AD, Einstein G, Gilbert J, Goedert M, Han SH, Huang D, Hulette C, Masliah E, Pericak-Vance MA, Saunders AM, Schmechel DE, Strittmatter WJ, Weisgraber KH, Xi PT (1996). "Morphological, biochemical, and genetic support for an apolipoprotein E effect on microtubular metabolism". Ann. N. Y. Acad. Sci. 777: 146–57. doi:10.1111/j.1749-6632.1996.tb34413.x. PMID 8624078.
- Snásel J, Pichová I (1997). "The cleavage of host cell proteins by HIV-1 protease". Folia Biol. (Praha). 42 (5): 227–30. doi:10.1007/BF02818986. PMID 8997639.
- Shafit-Zagardo B, Kalcheva N (1999). "Making sense of the multiple MAP-2 transcripts and their role in the neuron". Mol. Neurobiol. 16 (2): 149–62. doi:10.1007/BF02740642. PMID 9588626.
- Liu Y, Saad RS, Shen SS, Silverman JF (2003). "Diagnostic value of microtubule-associated protein-2 (MAP-2) for neuroendocrine neoplasms". Advances in Anatomic Pathology. 10 (2): 101–6. doi:10.1097/00125480-200303000-00005. PMID 12605092.
- Ainsztein AM, Purich DL (1992). "Cleavage of bovine brain microtubule-associated protein-2 by human immunodeficiency virus proteinase". J. Neurochem. 59 (3): 874–80. doi:10.1111/j.1471-4159.1992.tb08325.x. PMID 1494913.
- Alberts MJ, Kandt RS, Pericak-Vance MA, Bebout J, Speer MC, Siddique TS, Yamaoka L, Hung WY, Gaskell PC, Roses AD (1991). "MspI RFLP for microtubule associated protein-2 (MAP2)". Nucleic Acids Res. 19 (4): 960. doi:10.1093/nar/19.4.960. PMC 333743 . PMID 1708129.
- Wallin M, Deinum J, Goobar L, Danielson UH (1990). "Proteolytic cleavage of microtubule-associated proteins by retroviral proteinases". J. Gen. Virol. 71 (9): 1985–91. doi:10.1099/0022-1317-71-9-1985. PMID 2212989.
- Kosik KS, Orecchio LD, Bakalis S, Duffy L, Neve RL (1988). "Partial sequence of MAP2 in the region of a shared epitope with Alzheimer neurofibrillary tangles". J. Neurochem. 51 (2): 587–98. doi:10.1111/j.1471-4159.1988.tb01079.x. PMID 2455776.
- Dammerman M, Yen SH, Shafit-Zagardo B (1990). "Sequence of a human MAP-2 region sharing epitopes with Alzheimer neurofibrillary tangles". J. Neurosci. Res. 24 (4): 487–95. doi:10.1002/jnr.490240405. PMID 2481044.
- Obar RA, Dingus J, Bayley H, Vallee RB (1990). "The RII subunit of cAMP-dependent protein kinase binds to a common amino-terminal domain in microtubule-associated proteins 2A, 2B, and 2C". Neuron. 3 (5): 639–45. doi:10.1016/0896-6273(89)90274-2. PMID 2561973.
- Rubino HM, Dammerman M, Shafit-Zagardo B, Erlichman J (1990). "Localization and characterization of the binding site for the regulatory subunit of type II cAMP-dependent protein kinase on MAP2". Neuron. 3 (5): 631–8. doi:10.1016/0896-6273(89)90273-0. PMID 2701845.
- Herrmann H, Wiche G (1987). "Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin". J. Biol. Chem. 262 (3): 1320–5. PMID 3027087.
- Garner CC, Tucker RP, Matus A (1989). "Selective localization of messenger RNA for cytoskeletal protein MAP2 in dendrites". Nature. 336 (6200): 674–7. doi:10.1038/336674a0. PMID 3200318.
- Takahashi M, Tomizawa K, Sato K, Ohtake A, Omori A (1995). "A novel tau-tubulin kinase from bovine brain". FEBS Lett. 372 (1): 59–64. doi:10.1016/0014-5793(95)00955-9. PMID 7556643.
- Kindler S, Garner CC (1995). "Four repeat MAP2 isoforms in human and rat brain". Brain Res. Mol. Brain Res. 26 (1–2): 218–24. doi:10.1016/0169-328X(94)90093-0. PMID 7854050.
- Albala JS, Kalcheva N, Shafit-Zagardo B (1994). "Characterization of the transcripts encoding two isoforms of human microtubule-associated protein-2 (MAP-2)". Gene. 136 (1–2): 377–8. doi:10.1016/0378-1119(93)90502-T. PMID 8294038.
- Illenberger S, Drewes G, Trinczek B, Biernat J, Meyer HE, Olmsted JB, Mandelkow EM, Mandelkow E (1996). "Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics". J. Biol. Chem. 271 (18): 10834–43. doi:10.1074/jbc.271.18.10834. PMID 8631898.
- Björkblom B, Ostman N, Hongisto V, Komarovski V, Filén JJ, Nyman TA, Kallunki T, Courtney MJ, Coffey ET (2005). "Constitutively active cytoplasmic c-Jun N-terminal kinase 1 is a dominant regulator of dendritic architecture: role of microtubule-associated protein 2 as an effector". J. Neurosci. 25 (27): 6350–61. doi:10.1523/JNEUROSCI.1517-05.2005. PMID 16000625.
UpToDate Contents
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English Journal
- The effect of substrate topography on direct reprogramming of fibroblasts to induced neurons.
- Kulangara K1, Adler AF1, Wang H2, Chellappan M1, Hammett E1, Yasuda R3, Leong KW4.
- Biomaterials.Biomaterials.2014 Jul;35(20):5327-36. doi: 10.1016/j.biomaterials.2014.03.034. Epub 2014 Apr 4.
- Cellular reprogramming holds tremendous potential for cell therapy and regenerative medicine. Recently, fibroblasts have been directly converted into induced neurons (iNs) by overexpression of the neuronal transcription factors Ascl1, Brn2 and Myt1L. Hypothesizing that cell-topography interactions c
- PMID 24709523
- Neurogenin 2 Enhances the Neuronal Differentiation of Skin-derived Precursors.
- Dai X1, Lu X, Cheng F, Hao H, Qian T, Yu W, Tang L, Li L.
- The International journal of neuroscience.Int J Neurosci.2014 Jun 19:1-24. [Epub ahead of print]
- Abstracts Skin-derived precursors (SKPs), a novel stem cell population isolated from mammalian skin, can differentiate into neural and mesodermal lineages. Cell therapy using SKPs seems like a promising approach for the treatment of neural diseases, however, the low efficiency of neuronal differenti
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- The Synergistic Effect of Nanotopography and Sustained Dual Release of Hydrophobic and Hydrophilic Neurotrophic Factors on Human Mesenchymal Stem Cell Neuronal Lineage Commitment.
- Teo BK1, Tan GD, Yim EK.
- Tissue engineering. Part A.Tissue Eng Part A.2014 Jun 16. [Epub ahead of print]
- A combination of nanotopography and controlled release is a potential platform for neuronal tissue engineering applications. Previous studies showed that combining both physical and chemical guidance was more effective than individual cues in the directional promotion of neurite outgrowth. Nanotopog
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Japanese Journal
- Functional expression of carnitine/organic cation transporter OCTN1 in mouse brain neurons: Possible involvement in neuronal differentiation
- Nakamichi Noritaka,Taguchi Takayuki,Hosotani Hiroshi,Wakayama Tomohiko,Shimizu Takuya,Sugiura Tomoko,Iseki Shoichi,Kato Yukio
- Neurochemistry International 61(7), 1211-1132, 2012-12-00
- … Immunohistochemical analysis revealed colocalization of OCTN1 with neuronal cell markers microtubule-associated protein 2 (MAP2) and βIII-tubulin in mouse brain and primary cultured cortical neurons, respectively. …
- NAID 120004966621
- Rice Mitogen-Activated Protein Kinase Interactome Analysis Using the Yeast Two-Hybrid System
- Singh Raksha,Lee Mi-Ok,Lee Jae-Eun,Choi Jihyun,Park Ji Hun,Kim Eun Hye,Yoo Ran Hee,Cho Jung-Il,Jeon Jong-Seong,Rakwal Randeep,Agrawal Ganesh Kumar,Moon Jae Sun
- Plant physiology 160(1), 477-487, 2012-09-00
- … The established interactome contains four membrane-associated proteins, seven MAP2Ks (for MAPK kinase), four MAPKs, and 59 putative substrates, including 18 transcription factors. …
- NAID 120004754591
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- 英
- microtubule-associated protein 2、MAP2
- 関
- 微小管結合タンパク質
[★]
微小管結合タンパク質2
- 関
- MAP2、microtubule-associated protein
[★]
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