0000000000722839

AUTHOR

Pekka Roivas

0000-0001-6100-9533

showing 2 related works from this author

The Interaction Mechanism of Intrinsically Disordered PP2A Inhibitor Proteins ARPP-16 and ARPP-19 With PP2A

2021

Protein phosphatase 2A (PP2A) activity is critical for maintaining normal physiological cellular functions. PP2A is inhibited by endogenous inhibitor proteins in several pathological conditions including cancer. A PP2A inhibitor protein, ARPP-19, has recently been connected to several human cancer types. Accordingly, the knowledge about ARPP-19—PP2A inhibition mechanism is crucial for the understanding the disease development and the therapeutic targeting of ARPP-19—PP2A. Here, we show the first structural characterization of ARPP-19, and its splice variant ARPP-16 using NMR spectroscopy, and SAXS. The results reveal that both ARPP proteins are intrinsically disordered but contain transient…

macromolecular substancesIntrinsically disordered proteinsBiochemistry Genetics and Molecular Biology (miscellaneous)Biochemistryenvironment and public healthProtein–protein interactionprotein-protein interaction03 medical and health sciences0302 clinical medicineNMR spectroscopyIDPSARPP-16Molecular BiosciencesARPP-19NMR-spektroskopialcsh:QH301-705.5Molecular BiologyProtein secondary structure030304 developmental biologyOriginal Researchsoluviestintä0303 health sciencesMicroscale thermophoresisChemistryAlternative splicingInhibitor proteinProtein phosphatase 2Nuclear magnetic resonance spectroscopySAXS3. Good healthPP2APP2A inhibitor proteinssyöpäsolutlcsh:Biology (General)Biophysicsintrinsically disordered proteinsproteiinit030217 neurology & neurosurgery
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Interaction mechanism of endogenous PP2A inhibitor protein ENSA with PP2A

2022

The vast diversity of protein phosphatase 2A (PP2A) holoenzyme composition ensures its multifaceted role in the regulation of cellular growth and signal transduction. In several pathological conditions, such as cancer, PP2A is inhibited by endogenous inhibitor proteins. Several PP2A inhibitor proteins have been identified, one of which is α-endosulfine (ENSA). ENSA inhibits PP2A activity when it is phosphorylated at Ser67 by Greatwall (Gwl) kinase. The role of ENSA in PP2A inhibition is rather well characterized, but knowledge of the mechanism of inhibition is scarce. In this study, we have performed comprehensive structural characterization of ENSA, and its interaction with PP2A A- and var…

Gene isoformMitosisEndogenymacromolecular substancesProtein Serine-Threonine KinasesPP2A inhibitor protein010402 general chemistry01 natural sciencesBiochemistryenvironment and public health03 medical and health sciencesX-Ray DiffractionNeoplasmsScattering Small AngleHumansProtein Phosphatase 2DPsPhosphorylationNMR-spektroskopiaMolecular BiologyNuclear Magnetic Resonance Biomolecular030304 developmental biologyinhibiittoritsoluviestintä0303 health sciencesChemistryKinaseCell growthCell CycleCell BiologyProtein phosphatase 2Inhibitor proteinSAXSPhosphoproteinsNMR3. Good health0104 chemical sciencesCell biologyPP2Aenzymes and coenzymes (carbohydrates)ENSAPhosphorylationIntercellular Signaling Peptides and ProteinsproteiinitSignal transductionMicrotubule-Associated ProteinsProtein Processing Post-TranslationalSignal TransductionFEBS Journal
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