The sea urchin kinome: A first look

Bradham, Cynthia A.; Foltz, Kathy R.; Beane, Wendy S.; Arnone, Maria Ina; Rizzo, Francesca; Coffman, James A.; Mushegian, Arcady; Goel, Manisha; Morales, Julia; Genevière, Anne Marie; Lapraz, François; Robertson, A; Kelkar, Hemant; Loza-Coll, Mariano; Townley, Ian K.; Raisch, Michael; Roux, Michelle M.; Lepage, Thierry; Gache, Christian; McClay, David R.; Manning, Gerard

doi:10.1016/j.ydbio.2006.08.074

Cited by 82 publications

(72 citation statements)

References 94 publications

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“…PKC represents a large family of enzymes with at least 10 isoforms (Mellor and Parker, 1998). In the sea urchin, four different PKC genes have been found in the recently released Strongylocentrotes purpuratus genome (Bradham et al, 2006). The PKC inhibitors, as well as the antibodies used herein, can act (or react) on several mammalian PKC isoforms, and not necessarily with the same potency on each isoform.…”

Section: Discussionmentioning

confidence: 99%

Protein kinase C is an important signaling mediator associated with motility of intact sea urchin spermatozoa

White

Lamirande

Gagnon

2007

Journal of Experimental Biology

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SUMMARY Numerous kinases and phosphatases are most likely implicated in sperm motility initiation and maintenance. Data on these signaling molecules were mostly obtained from studies conducted on in vitrodemembranated–reactivated sperm models but are not necessarily representative of the in vivo situation. We therefore investigated the effect of a variety of cell-permeable chemicals, mostly kinase inhibitors,on the motility initiation and maintenance of intact sea urchin spermatozoa. Among the 20 substances tested, the protein kinase C (PKC) inhibitor chelerythrine was the most potent, arresting motility at concentrations starting from 1.5–2 μmol l–1. Motility was also inhibited by two other PKC inhibitors as well as staurosporine. Furthermore,these inhibitors prevented the motility-associated increase in phosphorylation of at least four PKC substrates. These phospho-PKC target proteins, as assessed with an antibody specific to phosphorylated motifs of PKC substrates,were found to be associated with the flagellum, either in the Triton X-100 soluble portion or the axoneme (Triton X-100 insoluble). A phosphorylated PKC-like enzyme was also detected by immunoblotting in the flagellum, as well as a significant 50 kDa PKC cleavage product. Taken together, the data strongly indicate for the first time that, in vivo, which means on intact spermatozoa, PKC is a key signaling mediator associated with the maintenance of sea urchin sperm motility.

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Section: Discussionmentioning

confidence: 99%

Protein kinase C is an important signaling mediator associated with motility of intact sea urchin spermatozoa

White

Lamirande

Gagnon

2007

Journal of Experimental Biology

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“…Moreover, an S. mansoni Syk-family PTK, TK4, has been identified that may play a role in germ cell development (Knobloch et al 2002). The importance of PTKs to schistosome development is not surprising given that these signalling enzymes regulate multiple physiological processes, including differentiation, in animals; indeed, the importance of protein kinases to development is highlighted by the recent finding that 85 % of sea urchin signalling kinases are expressed in the developing embryo (Bradham et al 2006). Genistein blocks the activity of multiple PTKs in S. mansoni miracidia (as demonstrated here by p-Tyr-100 blotting) so the effects observed in the present work are unlikely specific to a single PTK.…”

Section: Bmentioning

confidence: 99%

Specific tyrosine phosphorylation induced in Schistosoma mansoni miracidia by haemolymph from schistosome susceptible, but not resistant, Biomphalaria glabrata

Walker

Rollinson

2007

Parasitology

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S U M M A R YMolecular interplay during snail-schistosome interactions is poorly understood and there is much to discover concerning the effect of snail host molecules on molecular processes in schistosomes. Using the Biomphalaria glabrata -Schistosoma mansoni host-parasite system, the effects of exposure to haemolymph, derived from schistosome-resistant and susceptible snail strains, on protein tyrosine phosphorylation in miracidia have been investigated. Western blotting revealed several tyrosine phosphorylated proteins in this larval stage. Exposure of miracidia to haemolymph from susceptible snails for 60 min resulted in a striking, 5-fold, increase in the tyrosine phosphorylation of a 56 kDa (p56) S. mansoni protein. In contrast, haemolymph from resistant snails had little effect on protein tyrosine phosphorylation levels in miracidia. Confocal microscopy revealed that tyrosine phosphorylation was predominantly associated with proteins present in the tegument. Finally, treatment of miracidia with the tyrosine kinase inhibitor genistein significantly impaired their development into primary sporocysts. The results open avenues for research that focus on the potential importance of phosphop56 to the outcome of schistosome infection in snails, and the significance of protein tyrosine kinase-mediated signalling events to the transformation of S. mansoni larvae.

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“…Polo-like kinases (Plks) are found in all eukaryotes and are characterized by a highly conserved kinase domain and one or two C-terminal polo box domains (PBDs). These include the Plk1 subfamily, containing Drosophila polo and mammalian Plk1; the SAK subfamily, containing Drosophila SAK and mammalian Plk4, both of which are widely distributed across the eukaryotes; and the Plk2 subfamily, containing vertebrate Plk2 and Plk3 and also including homologs from echinoderms (4,8,10,35). The PBD participates in subcellular localization and partner interaction (16,54).…”

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confidence: 99%

Plk5, a Polo Box Domain-Only Protein with Specific Roles in Neuron Differentiation and Glioblastoma Suppression

Cárcer

Escobar

Higuero

et al. 2011

Molecular and Cellular Biology

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102

104

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Polo-like kinases (Plks) are characterized by the presence of a specific domain, known as the polo box (PBD), involved in protein-protein interactions. Plk1 to Plk4 are involved in centrosome biology as well as the regulation of mitosis, cytokinesis, and cell cycle checkpoints in response to genotoxic stress. We have analyzed here the new member of the vertebrate family, Plk5, a protein that lacks the kinase domain in humans. Plk5 does not seem to have a role in cell cycle progression; in fact, it is downregulated in proliferating cells and accumulates in quiescent cells. This protein is mostly expressed in the brain of both mice and humans, and it modulates the formation of neuritic processes upon stimulation of the brain-derived neurotrophic factor (BDNF)/nerve growth factor (NGF)-Ras pathway in neurons. The human PLK5 gene is significantly silenced in astrocytoma and glioblastoma multiforme by promoter hypermethylation, suggesting a tumor suppressor function for this gene. Indeed, overexpression of Plk5 has potent apoptotic effects in these tumor cells. Thus, Plk5 seems to have evolved as a kinase-deficient PBD-containing protein with nervous system-specific functions and tumor suppressor activity in brain cancer.

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The sea urchin kinome: A first look

Cited by 82 publications

References 94 publications

Protein kinase C is an important signaling mediator associated with motility of intact sea urchin spermatozoa

Protein kinase C is an important signaling mediator associated with motility of intact sea urchin spermatozoa

Specific tyrosine phosphorylation induced in Schistosoma mansoni miracidia by haemolymph from schistosome susceptible, but not resistant, Biomphalaria glabrata

Plk5, a Polo Box Domain-Only Protein with Specific Roles in Neuron Differentiation and Glioblastoma Suppression

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