A1 Journal article (refereed)
1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16) (2020)

Thapa, C. J., Haataja, T., Pentikäinen, U., & Permi, P. (2020). 1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16). Biomolecular NMR Assignments, 14(2), 227-231. https://doi.org/10.1007/s12104-020-09951-w

JYU authors or editors

Publication details

All authors or editors: Thapa, Chandan J.; Haataja, Tatu; Pentikäinen, Ulla; Permi, Perttu

Journal or series: Biomolecular NMR Assignments

ISSN: 1874-2718

eISSN: 1874-270X

Publication year: 2020

Volume: 14

Issue number: 2

Pages range: 227-231

Publisher: Springer

Publication country: Netherlands

Publication language: English

DOI: https://doi.org/10.1007/s12104-020-09951-w

Publication open access: Openly available

Publication channel open access: Partially open access channel

Publication is parallel published (JYX): https://jyx.jyu.fi/handle/123456789/69659

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: proteins; enzymes; cell signaling; NMR spectroscopy

Free keywords: assignments; cAMP-regulated phosphoprotein-19; HA-detection, intrinsically disordered protein; NMR spectroscopy

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Ministry reporting: Yes

Reporting Year: 2020

JUFO rating: 1