Microtubule-associated protein

From Proteopedia

Revision as of 09:33, 23 December 2025

spinqualitylabelsall models Human microtubule-associated protein light chain 3B (cyan) complex with sequestosome peptide (green) (PDB code 2zjd) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Structural highlights 4 3D Structures of microtubule-associated protein Function Microtubule-associated protein light chain 3 (LC3) is recruited to autophagosomal membranes during autophagy[1]. The human LC3B is cleaved after synthesis to expose a C-terminal glycine which binds via a phospholipid anchor to autophagosomal vesicle membranes during autophagy. Thus detection of LC3 is a reliable method for monitoring autophagy. The microtubule-associated proteins are classified as 2 types. Type 1 includes MAP1 and type 2 includes MAP2, MAP4 and Tau protein. MAP1 are classical microtubule-associated proteins which bind along microtubule lattice[2]. Tau protein is the principal component of the tangles found in Alzheimer's disease. It is hyperphosphorylated on serines and threonines[3]. 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[4]. 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[5]. Microtubule-associated protein SPM1 colocalizes to the subpellicular microtubule in the parasite Toxoplasma gondii [6]. Microtubule-associated protein Spiral2 is an Arabidopsis thaliana protein which facilitates the transition of microtubules from pause state to growth[7]. Disease Microtubule-associated protein Tau is associated with Alzheimer Disease. Tau forms abnormal aggregates in patients' tissues. Mutations in tau protein are associated with neurodegenerative diseases like frontotemporal dementia[8]. Structural highlights [9]. Water molecules are shown as red spheres. 3D Structures of microtubule-associated protein Microtubule-associated protein 3D structures

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. ↑ Tran JQ, Li C, Chyan A, Chung L, Morrissette NS. SPM1 stabilizes subpellicular microtubules in Toxoplasma gondii. Eukaryot Cell. 2012 Feb;11(2):206-16. PMID:22021240 doi:10.1128/EC.05161-11
7. ↑ Yao M, Wakamatsu Y, Itoh TJ, Shoji T, Hashimoto T. Arabidopsis SPIRAL2 promotes uninterrupted microtubule growth by suppressing the pause state of microtubule dynamics. J Cell Sci. 2008 Jul 15;121(Pt 14):2372-81. PMID:18577573 doi:10.1242/jcs.030221
8. ↑ 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
9. ↑ 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