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Unusual features and localization of the membrane kinome of Trypanosoma brucei.
- Source :
-
PloS one [PLoS One] 2021 Oct 15; Vol. 16 (10), pp. e0258814. Date of Electronic Publication: 2021 Oct 15 (Print Publication: 2021). - Publication Year :
- 2021
-
Abstract
- 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.<br />Competing Interests: The authors have declared that no competing interests exist.
- Subjects :
- Cell Membrane metabolism
Endoplasmic Reticulum metabolism
Epitopes immunology
Epitopes metabolism
Humans
Microscopy, Immunoelectron
Models, Molecular
Protein Conformation
Protein Domains
Protein Kinases immunology
Protozoan Proteins chemistry
Protozoan Proteins metabolism
Protein Kinases chemistry
Protein Kinases metabolism
Trypanosoma brucei brucei metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1932-6203
- Volume :
- 16
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- PloS one
- Publication Type :
- Academic Journal
- Accession number :
- 34653230
- Full Text :
- https://doi.org/10.1371/journal.pone.0258814