Microtubule-associated protein 2

Microtubule-associated protein 2
Identifiers
Symbols	MAP2 ; MAP2A; MAP2B; MAP2C
External IDs	OMIM: 157130 MGI: 97175 HomoloGene: 1779 GeneCards: MAP2 Gene
Gene ontology Molecular function • dystroglycan binding • structural molecule activity • protein binding • calmodulin binding • microtubule binding Cellular component • nucleolus • cytoplasm • smooth endoplasmic reticulum • rough endoplasmic reticulum • microtubule • microtubule associated complex • nuclear periphery • neuronal cell body • dendritic shaft • CA3 pyramidal cell dendrite • neuronal postsynaptic density Biological process • microtubule bundle formation • axonogenesis • central nervous system neuron development • neuron projection development • response to estradiol • response to progesterone • dendrite morphogenesis • cellular response to organic substance Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4133	17756
Ensembl	ENSG00000078018	ENSMUSG00000015222
UniProt	P11137	P20357
RefSeq (mRNA)	NM_001039538	NM_001039934
RefSeq (protein)	NP_001034627	NP_001035023
Location (UCSC)	Chr 2: 209.42 – 209.73 Mb	Chr 1: 66.18 – 66.44 Mb
PubMed search

Microtubule-associated protein 2 is a protein that in humans is encoded by the MAP2 gene.^[1][2]

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.^[3]

Interactions

MAP2 has been shown to interact with Grb2,^[4][5] NEFL^[6] and MYO7A.^[7] MAP2 is suspected of interacting with tubulin.

References

1. 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.
2. 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.
3. "Entrez Gene: MAP2 microtubule-associated protein 2".
4. 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.
5. 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.
6. Frappier T, Stetzkowski-Marden F, Pradel LA (April 1991). "Interaction domains of neurofilament light chain and brain spectrin". Biochem. J. 275 ( Pt 2) (Pt 2): 521–7. PMC 1150082. PMID 1902666.
7. 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 ( Pt 9) (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.