Microtubule-associated protein

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*'''MAP1''' are classical microtubule-associated proteins which bind along microtubule lattice<ref>PMID:16938900</ref>.<br />
*'''MAP1''' are classical microtubule-associated proteins which bind along microtubule lattice<ref>PMID:16938900</ref>.<br />
*'''Tau protein''' is the principal component of the tangles found in Alzheimer's disease. It is hyperphosphorylated on serines and threonines<ref>PMID:19542604</ref>.
*'''Tau protein''' is the principal component of the tangles found in Alzheimer's disease. It is hyperphosphorylated on serines and threonines<ref>PMID:19542604</ref>.
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*'''Microtubule-associated protein RP/EB family member 1''' (MAPRE1) is involved in the regulation of microtubule structure and chromosome stability. It associates with dynactin and the spindle during mitosis<ref>PMID:22919</ref>.
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*'''Microtubule-associated protein RP/EB family member 3''' (MAPRE3) localizes to the cytoplasmic microtubule network and binds a homolog of the adenomatous polyposis coli tumor suppressor gene<ref>PMID:22924</ref>.
== Disease ==
== Disease ==
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**[[4glr]], [[4tqe]], [[5dmg]] – hTau peptide + antibody<br />
**[[4glr]], [[4tqe]], [[5dmg]] – hTau peptide + antibody<br />
**[[4fl5]], [[4y32]], [[4y3b]], [[4y5i]] – hTau peptide + 14-3-3 protein σ<br />
**[[4fl5]], [[4y32]], [[4y3b]], [[4y5i]] – hTau peptide + 14-3-3 protein σ<br />
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*Microtubule-associated protein RP/EB family member 1
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**[[1wu9]] – hMAPRE1 C-terminal<br />
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**[[1yib]], [[1yig]] – hMAPRE1 C-terminal dimerization domain<br />
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**[[1vka]], [[2r8u]], [[1pa7]], [[1ueg]] – hMAPRE1 N-terminal<br />
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**[[2qjz]] – hMAPRE1 CH domain <br />
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**[[3gjo]] – hMAPRE1 C-terminal + dystonin peptide<br />
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**[[1txq]], [[2hkq]], [[2hl5]] – hMAPRE1 C-terminal + dynactin CAP-Gly domain<br />
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**[[3tq7]] – hMAPRE1 C-terminal + hRPEB member 3 C-terminal + dynactin CAP-Gly domain<br />
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*Microtubule-associated protein RP/EB family member 3
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**[[1v5k]] – mMAPRE3 CH domain - NMR<br />
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**[[3co1]] – hMAPRE3 CH domain <br />
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**[[1wyo]] – hMAPRE3 CH domain - NMR<br />
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**[[3jak]], [[3jal]], [[3gar]] – hMAPRE3 CH domain + tubulin + 3GTP – Cryo EM<br />
}}
}}

Revision as of 12:00, 10 December 2017

Human microtubule-associated protein light chain 3B (cyan) complex with sequestosome peptide (green) (PDB code 2zjd)

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3D Structures of microtubule-associated protein

Updated on 10-December-2017

References

  1. Maccioni RB, Cambiazo V. Role of microtubule-associated proteins in the control of microtubule assembly. Physiol Rev. 1995 Oct;75(4):835-64. PMID:7480164
  2. Halpain S, Dehmelt L. The MAP1 family of microtubule-associated proteins. Genome Biol. 2006;7(6):224. PMID:16938900
  3. Lebouvier T, Scales TM, Williamson R, Noble W, Duyckaerts C, Hanger DP, Reynolds CH, Anderton BH, Derkinderen P. The microtubule-associated protein tau is also phosphorylated on tyrosine. J Alzheimers Dis. 2009;18(1):1-9. doi: 10.3233/JAD-2009-1116. PMID:19542604 doi:http://dx.doi.org/10.3233/JAD-2009-1116
  4. Buligescu L, Lenkei R, Ciontea M, Dan EM. [Significance of anti-albumin antibodies in chronic liver disease]. Rev Med Interna Neurol Psihiatr Neurochir Dermatovenerol Med Interna. 1977, Jul-Aug;29(4):363-70. PMID:22919
  5. Turtola LO. Enamel microhardness and fluoride uptake underneath fermenting and non-fermenting artificial plaque. Scand J Dent Res. 1977 Sep;85(6):373-9. PMID:22924
  6. Schraen-Maschke S, Dhaenens CM, Delacourte A, Sablonniere B. Microtubule-associated protein tau gene: a risk factor in human neurodegenerative diseases. Neurobiol Dis. 2004 Apr;15(3):449-60. PMID:15056452 doi:http://dx.doi.org/10.1016/j.nbd.2003.12.009
  7. Ichimura Y, Kumanomidou T, Sou YS, Mizushima T, Ezaki J, Ueno T, Kominami E, Yamane T, Tanaka K, Komatsu M. Structural basis for sorting mechanism of p62 in selective autophagy. J Biol Chem. 2008 Aug 15;283(33):22847-57. Epub 2008 Jun 4. PMID:18524774 doi:http://dx.doi.org/M802182200

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