Unusual features and localization of the membrane kinome of Trypanosoma brucei.

In many eukaryotes, multiple protein kinases are situated in the plasma membrane where they respond to extracellular ligands. Ligand binding elicits a signal that is transmitted across the membrane, leading to activation of the cytosolic kinase domain. Humans have over 100 receptor protein kinases....

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Bryan C Jensen, Pashmi Vaney, John Flaspohler, Isabelle Coppens, Marilyn Parsons
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2021
Materias:
R
Q
Acceso en línea:https://doaj.org/article/7efbcf359f92496dbe1a2a31c390968d
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:7efbcf359f92496dbe1a2a31c390968d
record_format dspace
spelling oai:doaj.org-article:7efbcf359f92496dbe1a2a31c390968d2021-12-02T20:16:51ZUnusual features and localization of the membrane kinome of Trypanosoma brucei.1932-620310.1371/journal.pone.0258814https://doaj.org/article/7efbcf359f92496dbe1a2a31c390968d2021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0258814https://doaj.org/toc/1932-6203In many eukaryotes, multiple protein kinases are situated in the plasma membrane where they respond to extracellular ligands. Ligand binding elicits a signal that is transmitted across the membrane, leading to activation of the cytosolic kinase domain. Humans have over 100 receptor protein kinases. In contrast, our search of the Trypanosoma brucei kinome showed that there were only ten protein kinases with predicted transmembrane domains, and unlike other eukaryotic transmembrane kinases, seven are predicted to bear multiple transmembrane domains. Most of the ten kinases, including their transmembrane domains, are conserved in both Trypanosoma cruzi and Leishmania species. Several possess accessory domains, such as Kelch, nucleotide cyclase, and forkhead-associated domains. Surprisingly, two contain multiple regions with predicted structural similarity to domains in bacterial signaling proteins. A few of the protein kinases have previously been localized to subcellular structures such as endosomes or lipid bodies. We examined the localization of epitope-tagged versions of seven of the predicted transmembrane kinases in T. brucei bloodstream forms and show that five localized to the endoplasmic reticulum. The last two kinases are enzymatically active, integral membrane proteins associated with the flagellum, flagellar pocket, or adjacent structures as shown by both fluorescence and immunoelectron microscopy. Thus, these kinases are positioned in structures suggesting participation in signal transduction from the external environment.Bryan C JensenPashmi VaneyJohn FlaspohlerIsabelle CoppensMarilyn ParsonsPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 10, p e0258814 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Bryan C Jensen
Pashmi Vaney
John Flaspohler
Isabelle Coppens
Marilyn Parsons
Unusual features and localization of the membrane kinome of Trypanosoma brucei.
description In many eukaryotes, multiple protein kinases are situated in the plasma membrane where they respond to extracellular ligands. Ligand binding elicits a signal that is transmitted across the membrane, leading to activation of the cytosolic kinase domain. Humans have over 100 receptor protein kinases. In contrast, our search of the Trypanosoma brucei kinome showed that there were only ten protein kinases with predicted transmembrane domains, and unlike other eukaryotic transmembrane kinases, seven are predicted to bear multiple transmembrane domains. Most of the ten kinases, including their transmembrane domains, are conserved in both Trypanosoma cruzi and Leishmania species. Several possess accessory domains, such as Kelch, nucleotide cyclase, and forkhead-associated domains. Surprisingly, two contain multiple regions with predicted structural similarity to domains in bacterial signaling proteins. A few of the protein kinases have previously been localized to subcellular structures such as endosomes or lipid bodies. We examined the localization of epitope-tagged versions of seven of the predicted transmembrane kinases in T. brucei bloodstream forms and show that five localized to the endoplasmic reticulum. The last two kinases are enzymatically active, integral membrane proteins associated with the flagellum, flagellar pocket, or adjacent structures as shown by both fluorescence and immunoelectron microscopy. Thus, these kinases are positioned in structures suggesting participation in signal transduction from the external environment.
format article
author Bryan C Jensen
Pashmi Vaney
John Flaspohler
Isabelle Coppens
Marilyn Parsons
author_facet Bryan C Jensen
Pashmi Vaney
John Flaspohler
Isabelle Coppens
Marilyn Parsons
author_sort Bryan C Jensen
title Unusual features and localization of the membrane kinome of Trypanosoma brucei.
title_short Unusual features and localization of the membrane kinome of Trypanosoma brucei.
title_full Unusual features and localization of the membrane kinome of Trypanosoma brucei.
title_fullStr Unusual features and localization of the membrane kinome of Trypanosoma brucei.
title_full_unstemmed Unusual features and localization of the membrane kinome of Trypanosoma brucei.
title_sort unusual features and localization of the membrane kinome of trypanosoma brucei.
publisher Public Library of Science (PLoS)
publishDate 2021
url https://doaj.org/article/7efbcf359f92496dbe1a2a31c390968d
work_keys_str_mv AT bryancjensen unusualfeaturesandlocalizationofthemembranekinomeoftrypanosomabrucei
AT pashmivaney unusualfeaturesandlocalizationofthemembranekinomeoftrypanosomabrucei
AT johnflaspohler unusualfeaturesandlocalizationofthemembranekinomeoftrypanosomabrucei
AT isabellecoppens unusualfeaturesandlocalizationofthemembranekinomeoftrypanosomabrucei
AT marilynparsons unusualfeaturesandlocalizationofthemembranekinomeoftrypanosomabrucei
_version_ 1718374413723762688