Trypanosoma congolense: Developmental Regulation of Protein Kinases and Tyrosine Phosphorylation during the Life Cycle

1995 ◽  
Vol 80 (3) ◽  
pp. 507-514 ◽  
Author(s):  
M. Parsons ◽  
V. Carter ◽  
A. Muthiani ◽  
N. Murphy
Keyword(s):  
Life Cycle ◽  
Tyrosine Phosphorylation ◽  
Protein Kinases ◽  
Developmental Regulation ◽  
Trypanosoma Congolense

scholarly journals dDYRK2: a novel dual-specificity tyrosine-phosphorylation-regulated kinase in Drosophila

2003 ◽  
Vol 374 (2) ◽  
pp. 381-391 ◽  
Author(s):  
Pamela A. LOCHHEAD ◽  
Gary SIBBET ◽  
Ross KINSTRIE ◽  
Tava CLEGHON ◽  
Margie RYLATT ◽  
...  
Keyword(s):  
Tyrosine Phosphorylation ◽  
Protein Kinases ◽  
Mutational Analysis ◽  
Kinase Domain ◽  
Activation Loop ◽  
Embryonic Neurogenesis ◽  
Founding Family ◽  
Dual Specificity ◽  
Eukaryotic Organisms

Dual-specificity tyrosine-phosphorylation-regulated kinases (DYRKs) are an emerging family of protein kinases that have been identified in all eukaryotic organisms examined to date. DYRK family members are involved in regulating key developmental and cellular processes such as neurogenesis, cell proliferation, cytokinesis and cellular differentiation. Two distinct subgroups exist, nuclear and cytosolic. In Drosophila, the founding family member minibrain, whose human orthologue maps to the Down syndrome critical region, belongs to the nuclear subclass and affects post-embryonic neurogenesis. In the present paper, we report the isolation of dDYRK2, a cytosolic DYRK and the putative product of the smell-impaired smi35A gene. This is the second such kinase described in Drosophila, but the first to be characterized at the molecular and biochemical level. dDYRK2 is an 81 kDa dual-specificity kinase that autophosphorylates on tyrosine and serine/threonine residues, but appears to phosphorylate exogenous substrates only on serine/threonine residues. It contains a YXY motif in the activation loop of the kinase domain in the same location as the TXY motif in mitogenactivated protein kinases. dDYRK2 is tyrosine-phosphorylated in vivo, and mutational analysis reveals that the activation loop tyrosines are phosphorylated and are essential for kinase activity. Finally, dDYRK2 is active at all stages of fly development, with elevated levels observed during embryogenesis and pupation.

scholarly journals Mitochondrial Development during Life Cycle Differentiation of African Trypanosomes: Evidence for a Kinetoplast-dependent Differentiation Control Point

2002 ◽  
Vol 13 (10) ◽  
pp. 3747-3759 ◽  
Author(s):  
Mark W. Timms ◽  
Frederick J. van Deursen ◽  
Edward F. Hendriks ◽  
Keith R. Matthews
Keyword(s):  
Life Cycle ◽  
Rna Interference ◽  
Mitochondrial Genome ◽  
Topoisomerase Ii ◽  
Developmental Regulation ◽  
Control Point ◽  
Nuclear Genome ◽  
Mitochondrial Activity ◽  
African Trypanosomes

Life cycle differentiation of African trypanosomes entails developmental regulation of mitochondrial activity. This requires regulation of the nuclear genome and the kinetoplast, the trypanosome's unusual mitochondrial genome. To investigate the potential cross talk between the nuclear and mitochondrial genome during the events of differentiation, we have 1) disrupted expression of a nuclear-encoded component of the cytochrome oxidase (COX) complex; and 2) generated dyskinetoplastid cells, which lack a mitochondrial genome. Using RNA interference (RNAi) and by disrupting the nuclear COX VI gene, we demonstrate independent regulation of COX component mRNAs encoded in the nucleus and kinetoplast. However, two independent approaches (acriflavine treatment and RNA interference ablation of mitochondrial topoisomerase II) failed to establish clonal lines of dyskinetoplastid bloodstream forms. Nevertheless, dyskinetoplastid forms generated in vivo could undergo two life cycle differentiation events: transition from bloodstream slender to stumpy forms and the initiation of transformation to procyclic forms. However, they subsequently arrested at a specific point in this developmental program before cell cycle reentry. These results provide strong evidence for a requirement for kinetoplast DNA in the bloodstream and for a kinetoplast-dependent control point during differentiation to procyclic forms.

scholarly journals Complete In Vitro Life Cycle of Trypanosoma congolense: Development of Genetic Tools

2010 ◽  
Vol 4 (3) ◽  
pp. e618 ◽  
Author(s):  
Virginie Coustou ◽  
Fabien Guegan ◽  
Nicolas Plazolles ◽  
Théo Baltz
Keyword(s):  
Life Cycle ◽  
Trypanosoma Congolense ◽  
Genetic Tools

Developmental regulatin of RNA editing and polyadenylation in four life cycle stages of Trypanosoma congolense

1994 ◽  
Vol 68 (2) ◽  
pp. 297-306 ◽  
Author(s):  
Laurie K. Read ◽  
Kimberly A. Stankey ◽  
Wallace R. Fish ◽  
Anthony M. Muthiani ◽  
Kenneth Stuart
Keyword(s):  
Life Cycle ◽  
Rna Editing ◽  
Trypanosoma Congolense ◽  
Life Cycle Stages

scholarly journals Differential protein expression throughout the life cycle of Trypanosoma congolense, a major parasite of cattle in Africa

2011 ◽  
Vol 177 (2) ◽  
pp. 116-125 ◽  
Author(s):  
Brett A. Eyford ◽  
Tatsuya Sakurai ◽  
Derek Smith ◽  
Bianca Loveless ◽  
Christiane Hertz-Fowler ◽  
...  
Keyword(s):  
Life Cycle ◽  
Protein Expression ◽  
Trypanosoma Congolense ◽  
Differential Protein Expression ◽  
Differential Protein

scholarly journals Calcium in the Backstage of Malaria Parasite Biology

2021 ◽  
Vol 11 ◽  
Author(s):  
Lucas Silva de Oliveira ◽  
Marcos Rodrigo Alborghetti ◽  
Renata Garcia Carneiro ◽  
Izabela Marques Dourado Bastos ◽  
Rogerio Amino ◽  
...  
Keyword(s):  
Life Cycle ◽  
Protein Kinases ◽  
Malaria Parasite ◽  
Developmental Stages ◽  
Receptor Gene ◽  
Food Vacuole ◽  
Parasite Development ◽  
Cell Infection ◽  
Parasite Life Cycle ◽  
Downstream Signaling

The calcium ion (Ca2+) is a ubiquitous second messenger involved in key biological processes in prokaryotes and eukaryotes. In Plasmodium species, Ca2+ signaling plays a central role in the parasite life cycle. It has been associated with parasite development, fertilization, locomotion, and host cell infection. Despite the lack of a canonical inositol-1,4,5-triphosphate receptor gene in the Plasmodium genome, pharmacological evidence indicates that inositol-1,4,5-triphosphate triggers Ca2+ mobilization from the endoplasmic reticulum. Other structures such as acidocalcisomes, food vacuole and mitochondria are proposed to act as supplementary intracellular Ca2+ reservoirs. Several Ca2+-binding proteins (CaBPs) trigger downstream signaling. Other proteins with no EF-hand motifs, but apparently involved with CaBPs, are depicted as playing an important role in the erythrocyte invasion and egress. It is also proposed that a cross-talk among kinases, which are not members of the family of Ca2+-dependent protein kinases, such as protein kinases G, A and B, play additional roles mediated indirectly by Ca2+ regulation. This statement may be extended for proteins directly related to invasion or egress, such as SUB1, ERC, IMC1I, IMC1g, GAP45 and EBA175. In this review, we update our understanding of aspects of Ca2+-mediated signaling correlated to the developmental stages of the malaria parasite life cycle.

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