Identification of PIM1 substrates reveals a role for NDRG1 phosphorylation in prostate cancer cellular migration and invasion
Through a chemical genetics screen and phospho-proteomics, Ledet and Ruff et al identify substrates of the oncogenic kinase PIM1 in prostate cancer cells. They find that NDRG1 protein is destabilized by PIM1-mediated phosphorylation to reduce its metastasis suppressor function. These findings shed l...
Main Authors: | , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2021-01-01
|
Series: | Communications Biology |
Online Access: | https://doi.org/10.1038/s42003-020-01528-6 |
id |
doaj-80eaf72f1a91430f8ee15122bdc18eb3 |
---|---|
record_format |
Article |
spelling |
doaj-80eaf72f1a91430f8ee15122bdc18eb32021-01-10T12:41:26ZengNature Publishing GroupCommunications Biology2399-36422021-01-014111210.1038/s42003-020-01528-6Identification of PIM1 substrates reveals a role for NDRG1 phosphorylation in prostate cancer cellular migration and invasionRussell J. Ledet0Sophie E. Ruff1Yu Wang2Shruti Nayak3Jeffrey A. Schneider4Beatrix Ueberheide5Susan K. Logan6Michael J. Garabedian7Departments of Biochemistry and Molecular Pharmacology, New York University School of MedicineDepartments of Biochemistry and Molecular Pharmacology, New York University School of MedicineDepartments of Biochemistry and Molecular Pharmacology, New York University School of MedicineProteomics Laboratory, New York University School of MedicineDepartments of Biochemistry and Molecular Pharmacology, New York University School of MedicineDepartments of Biochemistry and Molecular Pharmacology, New York University School of MedicineDepartments of Biochemistry and Molecular Pharmacology, New York University School of MedicineDepartment of Urology, New York University School of MedicineThrough a chemical genetics screen and phospho-proteomics, Ledet and Ruff et al identify substrates of the oncogenic kinase PIM1 in prostate cancer cells. They find that NDRG1 protein is destabilized by PIM1-mediated phosphorylation to reduce its metastasis suppressor function. These findings shed light on the role of PIM1 in prostate cancer.https://doi.org/10.1038/s42003-020-01528-6 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Russell J. Ledet Sophie E. Ruff Yu Wang Shruti Nayak Jeffrey A. Schneider Beatrix Ueberheide Susan K. Logan Michael J. Garabedian |
spellingShingle |
Russell J. Ledet Sophie E. Ruff Yu Wang Shruti Nayak Jeffrey A. Schneider Beatrix Ueberheide Susan K. Logan Michael J. Garabedian Identification of PIM1 substrates reveals a role for NDRG1 phosphorylation in prostate cancer cellular migration and invasion Communications Biology |
author_facet |
Russell J. Ledet Sophie E. Ruff Yu Wang Shruti Nayak Jeffrey A. Schneider Beatrix Ueberheide Susan K. Logan Michael J. Garabedian |
author_sort |
Russell J. Ledet |
title |
Identification of PIM1 substrates reveals a role for NDRG1 phosphorylation in prostate cancer cellular migration and invasion |
title_short |
Identification of PIM1 substrates reveals a role for NDRG1 phosphorylation in prostate cancer cellular migration and invasion |
title_full |
Identification of PIM1 substrates reveals a role for NDRG1 phosphorylation in prostate cancer cellular migration and invasion |
title_fullStr |
Identification of PIM1 substrates reveals a role for NDRG1 phosphorylation in prostate cancer cellular migration and invasion |
title_full_unstemmed |
Identification of PIM1 substrates reveals a role for NDRG1 phosphorylation in prostate cancer cellular migration and invasion |
title_sort |
identification of pim1 substrates reveals a role for ndrg1 phosphorylation in prostate cancer cellular migration and invasion |
publisher |
Nature Publishing Group |
series |
Communications Biology |
issn |
2399-3642 |
publishDate |
2021-01-01 |
description |
Through a chemical genetics screen and phospho-proteomics, Ledet and Ruff et al identify substrates of the oncogenic kinase PIM1 in prostate cancer cells. They find that NDRG1 protein is destabilized by PIM1-mediated phosphorylation to reduce its metastasis suppressor function. These findings shed light on the role of PIM1 in prostate cancer. |
url |
https://doi.org/10.1038/s42003-020-01528-6 |
work_keys_str_mv |
AT russelljledet identificationofpim1substratesrevealsaroleforndrg1phosphorylationinprostatecancercellularmigrationandinvasion AT sophieeruff identificationofpim1substratesrevealsaroleforndrg1phosphorylationinprostatecancercellularmigrationandinvasion AT yuwang identificationofpim1substratesrevealsaroleforndrg1phosphorylationinprostatecancercellularmigrationandinvasion AT shrutinayak identificationofpim1substratesrevealsaroleforndrg1phosphorylationinprostatecancercellularmigrationandinvasion AT jeffreyaschneider identificationofpim1substratesrevealsaroleforndrg1phosphorylationinprostatecancercellularmigrationandinvasion AT beatrixueberheide identificationofpim1substratesrevealsaroleforndrg1phosphorylationinprostatecancercellularmigrationandinvasion AT susanklogan identificationofpim1substratesrevealsaroleforndrg1phosphorylationinprostatecancercellularmigrationandinvasion AT michaeljgarabedian identificationofpim1substratesrevealsaroleforndrg1phosphorylationinprostatecancercellularmigrationandinvasion |
_version_ |
1714950953746038784 |