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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== Structural highlights ==
== Structural highlights ==
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<scene name='70/708075/Cv/3'>LC3 recognizes a sequestosome peptide which is a preferred target for autophagy and binds at the surface of LC3</scene><ref>PMID:18524774</ref>. Water molecules shown as red spheres.
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<scene name='70/708075/Cv/5'>LC3 recognizes a sequestosome peptide which is a preferred target for autophagy and binds at the surface of LC3</scene><ref>PMID:18524774</ref>. Water molecules are shown as red spheres.
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</StructureSection>
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== 3D Structures of microtubule-associated protein ==
== 3D Structures of microtubule-associated protein ==
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[[Microtubule-associated protein 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*MAP1 light chain 3A
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**[[1ugm]], [[3eci]], [[3wal]], [[4zdv]]– hLC3A – human<br />
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**[[3wan]] – hLC3A/ATG13 LIR<br />
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**[[5dpr]], [[5dpw]] – hLC3A/PLEKHM1 LIR<br />
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**[[5cx3]], [[5d94]] – hLC3A + FYC01 LIR<br />
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*MAP1 light chain 3B
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**[[3vtu]], [[5xac]] – hLC3B<br />
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**[[1v49]] – hLC3B – NMR<br />
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**[[3vtv]], [[3vtw]] – hLC3B/optineurin (mutant)<br />
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**[[3wao]] – hLC3B/ATG13 LIR<br />
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**[[3x0w]] – hLC3B/PLEKHM1 LIR<br />
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**[[4waa]] – hLC3B/NIX LIR<br />
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**[[5ms6]], [[5xae]] – hLC3B/RAVZ LIR<br />
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**[[5v4k]] – hLC3B/NEDD4 LIR<br />
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**[[5dcn]] – hLC3B + TECPR2 LIR<br />
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**[[2lue]] – hLC3B + optineurin peptide<br />
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**[[2zjd]] – hLC3B + sequestosome p62 peptide<br />
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**[[5xad]] – hLC3B + peptide<br />
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**[[229x]], [[5gmv]] – hLC3B + FUNDC1 peptide<br />
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**[[5ms2]], [[5ms5]] – hLC3B + RAVZ<br />
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**[[5wrd]] – LC3B + FYVE peptide - mouse<br />
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**[[2z0d]], [[2z0e]], [[2zzp]] – rLC3B + hCysteine protease ATG4B – rat<br />
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**[[2k6q]] – rLC3B + sequestosome p62 peptide - NMR<br />
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*MAP1 light chain 3C
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**[[3wam]] – hLC3C<br />
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**[[2ncn]] – hLC3C - NMR<br />
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**[[3vvw]] – hLC3C + NDP52<br />
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**[[3w1y]] – hLC3C + ribosomal protein S10<br />
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**[[3wap]] – hLC3C/ATG13 LIR<br />
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**[[4eoy]] – LC3C (mutant) + ATG3 – ''Plasmodium falciparum''<br />
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*Microtubule-associated protein tau
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**[[2mz7]] – hTau residues 584-629 - NMR<br />
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**[[1i8h]] – hTau peptide + PIN1 WW domain - NMR<br />
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**[[2on9]], [[4e0n]], [[4e0o]], [[4e0m]], [[4np8]] – hTau peptide <br />
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**[[3ovl]] – hTau peptide + Orange G<br />
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**[[4glr]], [[4tqe]], [[5dmg]] – hTau peptide + antibody<br />
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**[[4fl5]], [[4y32]], [[4y3b]], [[4y5i]] – hTau peptide + 14-3-3 protein σ<br />
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}}
 
== References ==
== References ==
<references/>
<references/>
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[[Category:Topic Page]]

Current revision

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

Drag the structure with the mouse to rotate

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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