Interdependence of laforin and malin proteins for their stability and functions could underlie the molecular basis of locus heterogeneity in Lafora disease

Journal of biosciences

Rashmi Parihar¹  Pankaj Kumar Singh¹  Mamta Upadhyay¹  Shuchi Mittal¹  Subramaniam Ganesh1¹ 

[1] malin promotes its own degradation via auto-ubiquitination,$$

关键词: Epilepsy;    locus heterogeneity;    post-translational modification;    protein-protein interaction;   

DOI  :  

来源: Indian Academy of Sciences

【 摘 要 】

Lafora disease (LD), an autosomal recessive and fatal form of neurodegenerative disorder, is characterized by the presence of polyglucosan inclusions in the affected tissues including the brain. LD can be caused by defects either in the 𝐸𝑃𝑀2𝐴 gene coding for the laforin protein phosphatase or the 𝑁𝐻𝐿𝑅𝐶𝐼 gene coding for the malin ubiquitin ligase. Since the clinical symptoms of LD patients representing the two genetic groups are very similar and since malin is known to interact with laforin, we were curious to examine the possibility that the two proteins regulate each others function. Using cell biological assays we demonstrate here thatmalin promotes its own degradation via auto-ubiquitination,

【 授权许可】

Unknown