Targeting of parvulin interactors by diazirine mediated cross-linking discloses a cellular role of human Par14/17 in actin polymerization
| Autor: | Tina Gerdes, Mike Blueggel, Edisa Rehic, Farnusch Kaschani, Irina Michin, Anna Goehring, Markus Kaiser, Peter Bayer, Nina Schulze |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Gene isoform 030102 biochemistry & molecular biology Cytoskeleton organization Chemistry DNA repair Clinical Biochemistry Parvulin Biochemistry Actins Polymerization Transport protein Cell biology NIMA-Interacting Peptidylprolyl Isomerase 03 medical and health sciences 030104 developmental biology Diazomethane Humans Amino Acid Sequence Molecular Biology Biologie Actin Biogenesis Ribonucleoprotein |
| Popis: | The peptidyl-prolyl cis/trans isomerases (PPIases) Parvulin 14 (Par14) and Parvulin 17 (Par17) result from alternative transcription initiation of the PIN4 gene. Whereas Par14 is present in all metazoan, Par17 is only expressed in Hominidae. Par14 resides mainly within the cellular nucleus, while Par17 is translocated into mitochondria. Using photo-affinity labeling, cross-linking and mass spectrometry (MS) we identified binding partners for both enzymes from HeLa lysates and disentangled their cellular roles. Par14 is involved in biogenesis of ribonucleoprotein (RNP)-complexes, RNA processing and DNA repair. Its elongated isoform Par17 participates in protein transport/translocation and in cytoskeleton organization. Nuclear magnetic resonance (NMR) spectroscopy reveals that Par17 binds to β-actin with its N-terminal region, while both parvulins initiate actin polymerization depending on their PPIase activity as monitored by fluorescence spectroscopy. The knockdown (KD) of Par17 in HCT116 cells results in a defect in cell motility and migration. |
| Databáze: | OpenAIRE |
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