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H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16) Chandan J. Thapa1,2,3 · Tatu Haataja1 · Ulla Pentikäinen2,3 · Perttu Permi1,4  Received: 23 March 2020 / Accepted: 21 May 2020 © The Author(s) 2020

Abstract Protein Phosphatase 2A, PP2A, the principal Serine/threonine phosphatase, has major roles in broad range of signaling pathways that include regulation of cell cycle, cell proliferation and neuronal signaling. The loss of function of PP2A is linked with many human diseases, like cancer and neurodegenerative disorders. Protein phosphatase 2A (PP2A) functions as tumor suppressor and its tumor suppressor activity is inhibited by the overexpression of PP2A inhibitor proteins in most of the cancers. ARPP-19/ARPP-16 has been identified as one of the potential PP2A inhibitor proteins. Here, we report the resonance assignment of backbone 1H, 13C and 15N atoms of human ARPP-19 and ARPP-16 proteins. These chemical shift values can provide valuable information for the further study of the dynamics and interaction of ARPP-proteins to PP2A using NMR spectroscopy. Keywords  Assignments · cAMP-regulated phosphoprotein-19 · HA-detection, intrinsically disordered protein · NMR spectroscopy

Biological context cAMP regulated phosphoprotein-19 (ARPP-19), and its splice variant ARPP-16, were originally identified as substrates of the cAMP dependent protein kinase in neostriatum. ARPP-16 is highly expressed in neuronal cells, whereas, ARPP-19 is expressed ubiquitously (Horiuchi et al. 1990). In neuronal cells, ARPP-19 acts as bridge between nerve growth factor and post-transcriptional regulation of neuronal gene expression and controls the neuronal development and Electronic supplementary material  The online version of this article (doi:https​://doi.org/10.1007/s1210​4-020-09951​-w) contains supplementary material, which is available to authorized users. * Perttu Permi [email protected] 1



Department of Biological and Environmental Science, University of Jyvaskyla, Jyvaskyla, Finland

2



Institute of Biomedicine, University of Turku, Turku, Finland

3

Turku Bioscience, University of Turku and Åbo Akademi, Turku, Finland

4

Department of Chemistry, Nanoscience Center, University of Jyvaskyla, Jyvaskyla, Finland



plasticity (Irwin et al. 2002). The reduced expression of ARPP-19 is associated with neurological disorders like Alzheimer’s disease and Down’s syndrome (Kim et al. 2001). ARPP-19 and ARPP-16 also plays roles in the regulation of cell cycle. Recent studies have reported the role of ARPP-19 in the development and progression of several human cancer types, such as, breast cancer (Lü et al. 2015), hepatocellular carcinoma (Song et al. 2014) and human glioma (Jiang et al. 2016). Phosphorylation of ARPP-19 by the greatwall kinase (Gwl) promotes mitotic entry and maintenance of mitotic state by inhibiting PP2A (Andrade et al. 2017; Gharbi-Ayachi et al. 2010; Song et al. 2014). ARPPs phosphorylated by the MAST3 (Microtubule Associated Ser/ Thr ki

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