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The nuclear envelope protein, LAP1B, is a novel protein phosphatase 1 substrate.

Authors: Santos, Mariana  Rebelo, Sandra  Van Kleeff, Paula J M  Kim, Connie E  Dauer, William T  Fardilha, Margarida  da Cruz E Silva, Odete A  da Cruz E Silva, Edgar F 
Citation: Santos M, etal., PLoS One. 2013 Oct 7;8(10):e76788. doi: 10.1371/journal.pone.0076788. eCollection 2013.
Pubmed: (View Article at PubMed) PMID:24116158
DOI: Full-text: DOI:10.1371/journal.pone.0076788

Protein phosphatase 1 (PP1) binding proteins are quintessential regulators, determining substrate specificity and defining subcellular localization and activity of the latter. Here, we describe a novel PP1 binding protein, the nuclear membrane protein lamina associated polypeptide 1B (LAP1B), which interacts with the DYT1 dystonia protein torsinA. The PP1 binding domain in LAP1B was here identified as the REVRF motif at amino acids 55-59. The LAP1B:PP1 complex can be immunoprecipitated from cells in culture and rat cortex and the complex was further validated by yeast co-transformations and blot overlay assays. PP1, which is enriched in the nucleus, binds to the N-terminal nuclear domain of LAP1B, as shown by immunocolocalization and domain specific binding studies. PP1 dephosphorylates LAP1B, confirming the physiological relevance of this interaction. These findings place PP1 at a key position to participate in the pathogenesis of DYT1 dystonia and related nuclear envelope-based diseases.

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CRRD Object Information
CRRD ID: 14697725
Created: 2019-08-03
Species: All species
Last Modified: 2019-08-03
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.