microtubule-associated protein 2

微小管結合タンパク質2

関

MAP2、microtubule-associated protein

WordNet

1. having partial rights and privileges or subordinate status; "an associate member"; "an associate professor"
2. a person who joins with others in some activity or endeavor; "he had to consult his associate before continuing"
3. a person with subordinate membership in a society, institution, or commercial enterprise; "associates in the law firm bill at a lower rate than do partners"
4. any event that usually accompanies or is closely connected with another; "first was the lightning and then its thunderous associate"
5. make a logical or causal connection; "I cannot connect these two pieces of evidence in my mind"; "colligate these facts"; "I cannot relate these events at all" (同)tie_in, relate, link, colligate, link up, connect
6. any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
7. a microscopically small tubule

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1. 〈人〉'を'(…の)『仲間に加える』,(…に)連合させる《+『名』〈人〉+『with』+『名』》 / (…と)…'を'結びつけて考える(起こす)《+『名』+『with』+『名』》 / (…と)『仲間になる』,交際する《+『with』+『名』》 / (…と)合体する,提携する《+『with』+『名』》 / 『仲間』,『同僚』;組合員 / 準会員 / 付属物;連想されるもの / 連合した;仲間の,同僚の / 補助の,準…
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/04/11 12:18:58」(JST)

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Microtubule-associated protein 2
Culture of rat brain cells stained with antibody to MAP2 (green), Neurofilament NF-H (red) and DNA (blue). MAP2 is found in neuronal dendrites, while the neurofilament is found predominantly in axons.
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 • cytoplasm • microtubule • microtubule associated complex • nuclear periphery • neuronal cell body • dendritic shaft Biological process • microtubule bundle formation • axonogenesis • peptidyl-threonine phosphorylation • central nervous system neuron development • neuron projection development • 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: 210.29 – 210.6 Mb	Chr 1: 66.18 – 66.44 Mb
PubMed search	[1]	[2]

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

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 isforms have been described.

Interactions

MAP2 has been shown to interact with Grb2, NEFL and MYO7A. MAP2 is suspected of interacting with tubulin.

References

Further reading

• Roses AD, Einstein G, Gilbert J, Goedert M, Han SH, Huang D et al. (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 et al. (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 et al. (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 et al. (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

• A new function for glycine GlyT2 transporters: Stimulation of γ-aminobutyric acid release from cerebellar nerve terminals through GAT1 transporter reversal and Ca(2+) -dependent anion channels.

• Milanese M, Romei C, Usai C, Oliveri M, Raiteri L.Author information Department of Pharmacy, Pharmacology and Toxicology Section, University of Genoa, Genoa, Italy; Center of Excellence for Biomedical Research, University of Genoa, Genoa, Italy.AbstractGlycine GlyT2 transporters are localized on glycine-storing nerve endings. Their main function is to accumulate glycine to replenish synaptic vesicles. Glycine was reported to be costored with γ-aminobutyric acid (GABA) in cerebellar interneurons that may coexpress glycine and GABA transporters, and this is confirmed here by confocal microscopy analysis showing coexpression of GAT1 and GlyT2 transporters on microtubule-associated protein-2-positive synaptosomes. It was found that GABA uptake elicited glycine release from cerebellar nerve endings by various mechanisms. We investigated whether and by what mechanisms activation of glycine transporters could mediate release of GABA. Nerve endings purified from cerebellum were prelabeled with [(3) H]GABA and exposed to glycine. Glycine stimulated [(3) H]GABA release in a concentration-dependent manner. The glycine effect was insensitive to strychnine or to 5,7-dichlorokynurenate but it was abolished when GlyT2 transporters were blocked. About 20% of the evoked release was dependent on external Ca(2+) entered by reversal of plasmalemmal Na(+) /Ca(2+) exchangers. A significant portion of the GlyT2-mediated release of [(3) H]GABA (about 50% of the external Ca(2+) -independent release) occurred by reversal of GABA GAT1 transporters. Na(+) ions, reaching the cytosol during glycine uptake through GlyT2, activated mitochondrial Na(+) /Ca(2+) exchangers, causing an increase in cytosolic Ca(2+) , which in turn triggered a Ca(2+) -induced Ca(2+) release process at inositoltrisphosphate receptors. Finally, the increased availability of Ca(2+) in the cytosol allowed the opening of anion channels permeable to GABA. In conclusion, GlyT2 transporters not only take up glycine to replenish synaptic vesicles but can also mediate release of GABA by reversal of GAT1 and permeation through anion channels. © 2013 Wiley Periodicals, Inc.
• Journal of neuroscience research.J Neurosci Res.2014 Mar;92(3):398-408. doi: 10.1002/jnr.23321. Epub 2013 Nov 23.
• Glycine GlyT2 transporters are localized on glycine-storing nerve endings. Their main function is to accumulate glycine to replenish synaptic vesicles. Glycine was reported to be costored with γ-aminobutyric acid (GABA) in cerebellar interneurons that may coexpress glycine and GABA transporters, an
• PMID 24273061

• Rottlerin induces autophagy and apoptosis in prostate cancer stem cells via PI3K/Akt/mTOR signaling pathway.

• Kumar D1, Shankar S2, Srivastava RK3.Author information 1Department of Pharmacology, Toxicology and Therapeutics, and Medicine, The University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, 66160, USA. Electronic address: dkumar2@kumc.edu.2Department of Pathology and Laboratory Medicine, The University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, KS 66160, USA. Electronic address: sshankar@kumc.edu.3Department of Pharmacology, Toxicology and Therapeutics, and Medicine, The University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, 66160, USA. Electronic address: rsrivastava@kumc.edu.AbstractAutophagy plays an important role in cellular homeostasis through the disposal and recycling of cellular components. Cancer stem cells (CSCs) play major roles in cancer initiation, progression, and drug resistance. Rottlerin (Rott) is an active molecule isolated from Mallotus philippinensis, a medicinal plant used in Ayurvedic Medicine for anti-allergic and anti-helminthic treatments, demonstrates anticancer activities. However, the molecular mechanisms by which it induces autophagy in prostate CSCs have not been examined. The main objective of the paper was to examine the molecular mechanisms by which Rott induces autophagy in prostate CSCs. Autophagy was measured by the lipid modification of light chain-3 (LC3) and the formation of autophagosomes. Apoptosis was measured by flow cytometer analysis. The Western blot analysis was used to examine the effects of Rott on the expression of PI3K, phosphorylation of Akt, phosphorylation of mTOR, and phosphorylation of AMPK in pros CSCs. RNAi technology was used to inhibit the expression of Beclin-1 and ATG-7. Rott induced the lipid modification of light chain-3 (LC3) and the formation of autophagosomes after 24h of Rott treatment in prostate CSCs. Rott-treated prostate CSCs induced transition from LC3-I to LC3-II, a hall mark of autophagy. Rott also induced the expression of Atg5, Atg7, Atg12 and Beclin-1 proteins during autophagy. The knock-down of Atg7 and Beclin-1 blocked Rott-induced autophagy. Furthermore, Rott induced AMPK phosphorylation was blocked by 3-MA, Baf and CHX. In addition, inhibition of AMPK expression by shRNA blocked Rott induced autophagy. In conclusion, a better understanding of the biology of autophagy and the pharmacology of autophagy modulators has the potential for facilitating the development of autophagy-based therapeutic interventions for prostate cancer.
• Cancer letters.Cancer Lett.2014 Feb 28;343(2):179-89. doi: 10.1016/j.canlet.2013.10.003. Epub 2013 Oct 11.
• Autophagy plays an important role in cellular homeostasis through the disposal and recycling of cellular components. Cancer stem cells (CSCs) play major roles in cancer initiation, progression, and drug resistance. Rottlerin (Rott) is an active molecule isolated from Mallotus philippinensis, a medic
• PMID 24125861

• Evaluation of the effectiveness of Gaussian filtering in distinguishing punctate synaptic signals from background noise during image analysis.

• Iwabuchi S1, Kakazu Y1, Koh JY1, Harata NC2.Author information 1Department of Molecular Physiology and Biophysics, University of Iowa, Carver College of Medicine, Iowa City, IA, USA.2Department of Molecular Physiology and Biophysics, University of Iowa, Carver College of Medicine, Iowa City, IA, USA. Electronic address: charles-harata@uiowa.edu.AbstractBACKGROUND: Images in biomedical imaging research are often affected by non-specific background noise. This poses a serious problem when the noise overlaps with specific signals to be quantified, e.g. for their number and intensity. A simple and effective means of removing background noise is to prepare a filtered image that closely reflects background noise and to subtract it from the original unfiltered image. This approach is in common use, but its effectiveness in identifying and quantifying synaptic puncta has not been characterized in detail.
• Journal of neuroscience methods.J Neurosci Methods.2014 Feb 15;223:92-113. doi: 10.1016/j.jneumeth.2013.12.003. Epub 2013 Dec 12.
• BACKGROUND: Images in biomedical imaging research are often affected by non-specific background noise. This poses a serious problem when the noise overlaps with specific signals to be quantified, e.g. for their number and intensity. A simple and effective means of removing background noise is to pre
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Japanese Journal

• Influence of Ser/Pro-rich domain and kinase domain of double cortin-like protein kinase on microtubule-binding activity

• Nagamine Tadashi,Shimomura Sachiko,Sueyoshi Noriyuki [他]
• Journal of Biochemistry 149(5), 619-627, 2011-05
• NAID 40018787453

• Overexpression of Microtubule-Associated Protein-1 Light Chain 3 Is Associated with Melanoma Metastasis and Vasculogenic Mimicry

• HAN Chunrong,SUN Baocun,WANG Wei,CAI Wenjuan,LOU Dan,SUN Yan,ZHAO Xiulan
• Tohoku journal of experimental medicine 223(4), 243-251, 2011-04-01
• NAID 10027990490

Related Links

• Microtubule-associated protein 2 - UniProt

Phosphorylated at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing detachment from microtubules, and their disassembly (By similarity). Isoform 2/MAP2c is probably ...

• Map2 - Microtubule-associated protein 2 - Mus musculus (Mouse)

Microtubule-associated protein 2 Short name: MAP-2 Gene names i Name:Map2 Synonyms: Mtap2 Organism i Mus musculus (Mouse) Taxonomic identifier i 10090 [NCBI] Taxonomic lineage i › Eukaryota ...

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リンク元	「微小管結合タンパク質2」「MAP2」
関連記事	「associate」「associated」「associated protein」

「微小管結合タンパク質2」

　　[★]

英

microtubule-associated protein 2、MAP2

関

微小管結合タンパク質

「MAP2」

　　[★]

微小管結合タンパク質2

関

microtubule-associated protein 2

「associate」

　　[★]

• vt.

• 結合する、連合させる。連想によって結びつける。(人を)仲間/友達などとしての関係に置く。(化)会合させる

• vi.

• 仲間/友人などとして交際する(with)。一つにまとめる、連合する

• n.

• 仕事仲間、提携者、同僚。友人、朋友。準会員。従業員、社員
• 密接な蒸す偽付きのある物、付随する物、つきもの。準国家
• 連想によって心に浮かぶ言葉/思い、連想物

• adj.

• 仲間の、同僚の。製紙機械員に次ぐ資格の
• 付随する、連想される

関

accompany、association、associative、attach、bearing、bind、binding、bond、bonding、coassemble、colleague、combine、conjoin、conjugate、conjugation、conjunction、connect、connection、correlate、correlation、couple、dock、engage、engagement、federation、implication、join、joint、ligate、link、linkage、peer、pertinent、reference、relate、relation、relationship、relative、relevance、relevant、symphysial、union

　 　 　 　 　 　

「associated」

　　[★]

• adj.

• 随伴の、随伴性の

関

concomitant、erratic、erratically

associate

「associated protein」

　　[★]

• 関連タンパク質

関

related protein