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The laforin/malin E3-ubiquitin ligase complex ubiquitinates pyruvate kinase M1/M2
|Authors:||Viana, Rosa ; Luján, Pablo; Sanz, Pascual|
|Citation:||BMC Biochemistry 16(1): 24 (2015)|
|Abstract:||[Background] Lafora disease (LD, OMIM 254780) is a fatal neurodegenerative disorder produced mainly by mutations in two genes: EPM2A, encoding the dual specificity phosphatase laforin, and EPM2B, encoding the E3-ubiquitin ligase malin. Although it is known that laforin and malin may form a functional complex, the underlying molecular mechanisms of this pathology are still far from being understood.|
[Methods] In order to gain information about the substrates of the laforin/malin complex, we have carried out a yeast substrate-trapping screening, originally designed to identify substrates of protein tyrosine phosphatases. [Results] Our results identify the two muscular isoforms of pyruvate kinase (PKM1 and PKM2) as novel interaction partners of laforin.
[Conclusions] We present evidence indicating that the laforin/malin complex is able to interact with and ubiquitinate both PKM1 and PKM2. This post-translational modification, although it does not affect the catalytic activity of PKM1, it impairs the nuclear localization of PKM2.
|Publisher version (URL):||http://dx.doi.org/10.1186/s12858-015-0053-6|
|Appears in Collections:||(IBV) Artículos|