Journals / Experimed / 2017 / Cilt: 7 - Sayı: 13

Neurodegenerative Diseases andSUMO

Nörodejeneratif Hastalıklar Ve SUMO

Journal
Experimed
Pages
59–70
Publication Date
2017-06-01
DOI
—
🏛️Bibliographic metadata and full text access for this article are provided via DergiPark.
DergiPark Record ↗
✨

AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

In the scope of this review, firstlyinformations about the SUMO proteins and sumoylation will be explained, thereafter informations onrelations between SUMO proteins and neurodegenerative diseases related to polyglutamine disorderrelated diseases, neuronal intranuclear inclusion disease, Parkinson’s disease and Alzheimer’s diseasewill be given.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:In this review, it will be focused on the functions of SUMO (Small ubiquitin-like modifiers) proteins,which are increasingly important in the pathophysiology of neurodegenerative diseases, on the diseasemechanisms.
📊
Key Findings & Data:Recyclable covalent bonds createdby one of SUMOs’ (in mammals are defined as SUMO1, SUMO2, SUMO3, SUMO4) lysin remains fromtarget proteins and impairments in the sumoylation cycle are associated with many neurological disorders.The identification of Huntingtin, ataxin-1, tau and α-synuclein as SUMO substrates leads to anassociation between sumoylation and neurodegenerative diseases.
💡
Conclusion & Impact:In the scope of this review, firstlyinformations about the SUMO proteins and sumoylation will be explained, thereafter informations onrelations between SUMO proteins and neurodegenerative diseases related to polyglutamine disorderrelated diseases, neuronal intranuclear inclusion disease, Parkinson’s disease and Alzheimer’s diseasewill be given.
🔬Design:Review & Systematic Survey
📍Scope:Comprehensive Sample
⚙️Variables:SUMO ve sumolasyon · Poliglutamin hastalıklar · Alzheimer hastalığı

Abstract

In this review, it will be focused on the functions of SUMO (Small ubiquitin-like modifiers) proteins,which are increasingly important in the pathophysiology of neurodegenerative diseases, on the diseasemechanisms. SUMO proteins play a crucial role in cellular processes. Recyclable covalent bonds createdby one of SUMOs’ (in mammals are defined as SUMO1, SUMO2, SUMO3, SUMO4) lysin remains fromtarget proteins and impairments in the sumoylation cycle are associated with many neurological disorders.The identification of Huntingtin, ataxin-1, tau and α-synuclein as SUMO substrates leads to anassociation between sumoylation and neurodegenerative diseases. In the scope of this review, firstlyinformations about the SUMO proteins and sumoylation will be explained, thereafter informations onrelations between SUMO proteins and neurodegenerative diseases related to polyglutamine disorderrelated diseases, neuronal intranuclear inclusion disease, Parkinson’s disease and Alzheimer’s diseasewill be given.

Özet

Bu derlemede nörodejeneratif hastalıkların patofizyolojisinde önemi gittikçe daha da artan SUMO(Small ubiquitin-like modifiers) proteinlerinin hastalıkların mekanizmasındaki işlevleri üzerinde durulacaktır.SUMO proteinleri hücresel proseslerde önemli ölçüde rol oynamaktadır. SUMO ailesinden(memelilerde dört farklı SUMO tanımlanmıştır: SUMO1, SUMO2, SUMO3, SUMO4) herhangi birinin hedefproteinlerdeki lizin kalıntılarıyla oluşturdukları geri dönüşümlü kovalent bağlar sumolasyon işlemiolarak bilinmektedir ve sumolasyon döngüsünde meydana gelen bozulmalar birçok nörolojik bozuklukile ilişkilendirilmiştir. Huntingtin, ataksin-1, tau ve α-sinükleinin SUMO substratları olarak tanımlanmasısumolasyon ve nörodejeneratif hastalıklar arasındaki ilişkiyi destekler yöndedir. Bu derleme kapsamındailk önce SUMO proteinleri ve sumolasyon hakkında bilgi verilecek daha sonra nörodejeneratifhastalıklardan poliglutamin bozukluğuyla ilişkili hastalıkların, nöronal intranükleer inklüzyon hastalığının,Parkinson hastalığının ve Alzheimer hastalığın SUMO proteinleri ile olan ilişkisine yönelik güncelbilgiler aktarılacaktır.

🔖

Cite This Article

Ay, U., Şen, M., Akbayır, E., Tüzün, E., Küçükali, C. İ. (2017). Neurodegenerative Diseases andSUMO. Experimed, Cilt: 7 - Sayı: 13, 59–70. https://ajindex.com/articles/50879

📄 Full Text PDF Viewer

📄

PDF görüntüleyici hazırlanıyor...

References (13)

  1. Anderson DB, Zanella CA, Henley JM, Cimarotsi H. Sumoylation: Implications for Neurode-generative Diseases. Adv Exp Med Biol 2017; 963: 261-281
  2. Dorval V, Fraser PE. SUMO on the road to neurodegeneration. Biochim Biophys Acta 2007;1773: 694-706
  3. Li M, Guo D, Isales CM., Eizirik DL, Atkinson M, She JX, Wang CY. Sumo wrestling with type 1 diabetes. J Mol Med 2005; 83: 504- 513
  4. Wang CY, SHE JX. SUMO4 and its role in type 1 diabetes pathogenesis. Diabetes Metab Res Rev 2008; 24: 93–102
  5. Bohren KM, nadkarni V, Song JH, Gabbay KH,Owerbach, D. A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus. J Biol Chem 2004; 279: 27233–27238
  6. Rodriguez MS, Desterro JM, Lain S, Midgley CA, Lane DP, Hay RT. SUMO-1 modification activates the transcriptional response of p53. EMBO J 1999; 15: 6455-6461
  7. Tatham MH, Jaffray E, Vaughan OA, Desterro JMP, Botting CH, Naismith JH, Hay RT. Polymeric Chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/ SAE2 and Ubc9. J Bio Chem 2001; 276(38): 35368-35374
  8. Wilkinson KA, Henley JM. Mechanisms, regulation and consequences of protein SUMOylation Biochem J 2012; 428(2): 133-145
  9. Martin S, Wilkinson KA, Nishimune A, Henly JM. Emergng exracellular roles of protein SUMOylation in neuronal function and dysfunction. Nat Rev Neurosci 2007; 8(12): 948- 959
  10. Song J, Durrin LK, Wilkinson TA, Krontiris TG, Chen Y. Identification of a SUMO-binding motif that recognizes SUMO-modified proteins. Proc Natl Acad Sci 2004; 101: 14373-14378 11. Slow EF, Graham RF, Osmand AP,Devon RS, Lu G, Deng Y, Pearson J, Vaid K, Bissada N, Wetzel R, Leavitt BR, Hayden MR, Absence of behavioral abnormalities and neurodegeneration in vivo despite widespread neuronal huntingtin inclusions. Proc Natl Acad Sci USA 2005; 102: 11402–11407
  11. Krumova P, Weishaupt JH. Sumoylation in neurodegenerative diseases. Cell Mol Life Sci 2013; 70: 2123-2138
  12. Bowman AB, Yoo SY, Dantuma NP, Zoghbi HY. Neuronaldysfunction in a polyglutamine disease model occurs in the absence ofubiquitin– proteasome system impairment and inversely correlates withthe degree of nuclear inclusion formation. Hum Mol Genet 2005; 14: 679-691
  13. Steffan JS, Agrawal N, Pallos J, Rockabrand E, Trotman LC, Slepko N, Illes K, Lukacsovich T, Zhu Y-Z, Cattaneo E, Pandolfi P,Thompson LM, Marsh JL. SUMO modification of Huntingtin andHuntington’s