CLK1/CLK2-driven signalling at the Leishmania kinetochore is captured by spatially referenced proximity phosphoproteomics
Combination of proximity biotinylation and protein cross-linking allows proximity phosphoproteomics of the kinetochore in Leishmania parasites during the cell cycle and captures perturbations at the kinetochore after treatment with a protein kinase inhibitor.
Main Authors: | , , , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2022-11-01
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Series: | Communications Biology |
Online Access: | https://doi.org/10.1038/s42003-022-04280-1 |
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author | Vincent Geoghegan Juliana B. T. Carnielli Nathaniel G. Jones Manuel Saldivia Sergios Antoniou Charlotte Hughes Rachel Neish Adam Dowle Jeremy C. Mottram |
author_facet | Vincent Geoghegan Juliana B. T. Carnielli Nathaniel G. Jones Manuel Saldivia Sergios Antoniou Charlotte Hughes Rachel Neish Adam Dowle Jeremy C. Mottram |
author_sort | Vincent Geoghegan |
collection | DOAJ |
description | Combination of proximity biotinylation and protein cross-linking allows proximity phosphoproteomics of the kinetochore in Leishmania parasites during the cell cycle and captures perturbations at the kinetochore after treatment with a protein kinase inhibitor. |
first_indexed | 2024-04-12T04:06:30Z |
format | Article |
id | doaj.art-8ed4bba9584b41d385a7ad7f0d9506f1 |
institution | Directory Open Access Journal |
issn | 2399-3642 |
language | English |
last_indexed | 2024-04-12T04:06:30Z |
publishDate | 2022-11-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Communications Biology |
spelling | doaj.art-8ed4bba9584b41d385a7ad7f0d9506f12022-12-22T03:48:36ZengNature PortfolioCommunications Biology2399-36422022-11-015111710.1038/s42003-022-04280-1CLK1/CLK2-driven signalling at the Leishmania kinetochore is captured by spatially referenced proximity phosphoproteomicsVincent Geoghegan0Juliana B. T. Carnielli1Nathaniel G. Jones2Manuel Saldivia3Sergios Antoniou4Charlotte Hughes5Rachel Neish6Adam Dowle7Jeremy C. Mottram8York Biomedical Research Institute and Department of Biology, University of YorkYork Biomedical Research Institute and Department of Biology, University of YorkYork Biomedical Research Institute and Department of Biology, University of YorkNovartis Institute for Tropical DiseasesYork Biomedical Research Institute and Department of Biology, University of YorkYork Biomedical Research Institute and Department of Biology, University of YorkYork Biomedical Research Institute and Department of Biology, University of YorkBioscience Technology Facility, Department of Biology, University of YorkYork Biomedical Research Institute and Department of Biology, University of YorkCombination of proximity biotinylation and protein cross-linking allows proximity phosphoproteomics of the kinetochore in Leishmania parasites during the cell cycle and captures perturbations at the kinetochore after treatment with a protein kinase inhibitor.https://doi.org/10.1038/s42003-022-04280-1 |
spellingShingle | Vincent Geoghegan Juliana B. T. Carnielli Nathaniel G. Jones Manuel Saldivia Sergios Antoniou Charlotte Hughes Rachel Neish Adam Dowle Jeremy C. Mottram CLK1/CLK2-driven signalling at the Leishmania kinetochore is captured by spatially referenced proximity phosphoproteomics Communications Biology |
title | CLK1/CLK2-driven signalling at the Leishmania kinetochore is captured by spatially referenced proximity phosphoproteomics |
title_full | CLK1/CLK2-driven signalling at the Leishmania kinetochore is captured by spatially referenced proximity phosphoproteomics |
title_fullStr | CLK1/CLK2-driven signalling at the Leishmania kinetochore is captured by spatially referenced proximity phosphoproteomics |
title_full_unstemmed | CLK1/CLK2-driven signalling at the Leishmania kinetochore is captured by spatially referenced proximity phosphoproteomics |
title_short | CLK1/CLK2-driven signalling at the Leishmania kinetochore is captured by spatially referenced proximity phosphoproteomics |
title_sort | clk1 clk2 driven signalling at the leishmania kinetochore is captured by spatially referenced proximity phosphoproteomics |
url | https://doi.org/10.1038/s42003-022-04280-1 |
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