ArticlePloS one2013
The nuclear envelope protein, LAP1B, is a novel protein phosphatase 1 substrate.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Comparing In vitro Protein Aggregation Modelling Using Strategies Relevant to Neuropathologies.Cellular and molecular neurobiology · 2025Article
- LAP1 Interactome Profiling Provides New Insights into LAP1's Physiological Functions.International journal of molecular sciences · 2024Article
- Quantitative proteome analysis of LAP1-deficient human fibroblasts: A pilot approach for predicting the signaling pathways deregulated in LAP1-associated diseases.Biochemistry and biophysics reports · 2024Article
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- Nuclear Accumulation of LAP1:TRF2 Complex during DNA Damage Response Uncovers a Novel Role for LAP1.Cells · 2020Article
- Descriptive Analysis of LAP1 Distribution and That of Associated Proteins throughout Spermatogenesis.Membranes · 2017Article
- Lamina-associated polypeptide 1 is dispensable for embryonic myogenesis but required for postnatal skeletal muscle growth.Human molecular genetics · 2017Article
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- Synphilin-1A is a phosphoprotein phosphatase 1-interacting protein and affects PPP1 sorting to subcellular compartments.Journal of molecular neuroscience : MN · 2015Article
- LAP1 is a crucial protein for the maintenance of the nuclear envelope structure and cell cycle progression.Molecular and cellular biochemistry · 2015Article
- Lamina-associated polypeptide 1: protein interactions and tissue-selective functions.Seminars in cell & developmental biology · 2014Review
- Identification of a novel human LAP1 isoform that is regulated by protein phosphorylation.PloS one · 2014Article
- Depletion of lamina-associated polypeptide 1 from cardiomyocytes causes cardiac dysfunction in mice.Nucleus (Austin, Tex.)Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
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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