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. 2011 Jul 28;11:225. doi: 10.1186/1471-2148-11-225

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Copyright ©2011 Romá-Mateo et al; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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The laforin-malin complex does not ubiquitinate TRIM32-related substrates such as dysbindin and PIASy. A) Ubiquitination of dysbindin. HEK293 cells were transfected with 6xHis-tagged ubiquitin construct, pmyc-dysbindin and plasmids encoding TRIM32 [wild type or a catalytically inactive form (H42A)] or plasmids encoding laforin and malin (pCMV-HA-laforin and pCDNA3-HA-malin). Samples were processed and analyzed as in Figure 6. Crude extracts were also analyzed for the presence of laforin and malin using an anti-HA antibody. B) Ubiquitination of PIASy. Similar experiments as those performed in part A) were conducted in cells expressing myc-PIASy. In addition we probed the action of Mdm2, another E3-ubiquitin ligase. Crude extracts were analyzed for the presence of laforin and malin using an anti-HA antibody, and with an anti-Mdm2.