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.

Bibliographic Details
Main Authors: Vincent Geoghegan, Juliana B. T. Carnielli, Nathaniel G. Jones, Manuel Saldivia, Sergios Antoniou, Charlotte Hughes, Rachel Neish, Adam Dowle, Jeremy C. Mottram
Format: Article
Language:English
Published: Nature Portfolio 2022-11-01
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.
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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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