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Title

Ubiquitin conjugating enzyme E2-N and sequestosome-1 (p62) are components of the ubiquitination process mediated by the malin-laforin E3-ubiquitin ligase complex

AuthorsSánchez-Martín, Pablo; Romá-Mateo, Carlos ; Viana, Rosa ; Sanz, Pascual
KeywordsUBE2N
E2-conjugase
p62 (SQSTM1)
Ubiquitination
E3-ubiquitin ligase
Malin
Laforin
Autophagosome
LC3
Issue Date3-Nov-2015
PublisherElsevier
CitationInternational Journal of Biochemistry and Cell Biology 69:204-14 (2015)
AbstractLafora disease (LD, OMIM254780, ORPHA501) is a rare neurodegenerative form of epilepsy related to mutations in two proteins: laforin, a dual specificity phosphatase, and malin, an E3-ubiquitin ligase. Both proteins form a functional complex, where laforin recruits specific substrates to be ubiquitinated by malin. However, little is known about the mechanism driving malin-laforin mediated ubiquitination of its substrates. In this work we present evidence indicating that the malin-laforin complex interacts physically and functionally with the ubiquitin conjugating enzyme E2-N (UBE2N). This binding determines the topology of the chains that the complex is able to promote in the corresponding substrates (mainly K63-linked polyubiquitin chains). In addition, we demonstrate that the malin-laforin complex interacts with the selective autophagy adaptor sequestosome-1 (p62). Binding of p62 to the malin-laforin complex allows its recognition by LC3, a component of the autophagosomal membrane. In addition, p62 enhances the ubiquitinating activity of the malin-laforin E3-ubiquitin ligase complex. These data enrich our knowledge on the mechanism of action of the malin-laforin complex as an E3-ubiquitin ligase and reinforces the role of this complex in targeting substrates towards the autophagy pathway.
Description11 páginas, 9 figuras.
Publisher version (URL)http://dx.doi.org/10.1016/j.biocel.2015.10.030
URIhttp://hdl.handle.net/10261/131005
DOI10.1016/j.biocel.2015.10.030
ISSN1357-2725
E-ISSN1878-5875
Appears in Collections:(IBV) Artículos
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