Divalent cation hinder the solubilization of a tubulin kinase activity from Trypanosoma cruzi epimastigotes

Trypanosoma cruzi epimastigotes were extracted under various conditions in order to examine the role of divalent cations in the solubilization of microtubule proteins. When epimastigotes were homogenized in the presence of 5 mM Mg+2 and 5 mM Ca+2, a protein kinase responsible for phosphorylating tub...

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Autores principales:	UZCANGA,GRACIELA, GALÁN-CARIDAD,JOSÉ MANUEL, SUAREZ,KAREM NORIS, BUBIS,JOSÉ
Lenguaje:	English
Publicado:	Sociedad de Biología de Chile 2003
Materias:	microtubules post-translational modification of tubulin protein kinase CK2 protein phosphorylation-dephosphorylation signal transduction Trypanosoma cruzi tubulin
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602003000300008
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spelling	oai:scielo:S0716-976020030003000082004-08-17Divalent cation hinder the solubilization of a tubulin kinase activity from Trypanosoma cruzi epimastigotesUZCANGA,GRACIELAGALÁN-CARIDAD,JOSÉ MANUELSUAREZ,KAREM NORISBUBIS,JOSÉ microtubules post-translational modification of tubulin protein kinase CK2 protein phosphorylation-dephosphorylation signal transduction Trypanosoma cruzi tubulin Trypanosoma cruzi epimastigotes were extracted under various conditions in order to examine the role of divalent cations in the solubilization of microtubule proteins. When epimastigotes were homogenized in the presence of 5 mM Mg+2 and 5 mM Ca+2, a protein kinase responsible for phosphorylating tubulin, as well as the tubulin that became phosphorylated, remained tightly associated with the parasite particulate and detergent-resistant fractions. On the contrary, tubulin kinase and its substrate were predominantly released into the parasite cytosolic and detergent-soluble fractions, when epimastigotes were extracted in the presence of 5 mM EDTA and 5 mM EGTA. These evidences demonstrated a divalent cation-dependent solubilization of the enzyme responsible for the phosphorylation of tubulin in T. cruzi epimastigotes and suggested a tight association between tubulin and this kinase. Under all conditions tested, tubulin kinase activity in epimastigote extracts was lower than the addition of the corresponding value in the parasite cytosolic and membranous fractions, suggesting the presence of a kinase inhibitor or regulatory subunit which also seemed to be modulated by divalent cations. Additionally, inhibition experiments in the presence of heparin, 2,3-bisphosphoglycerate and GTP established that the parasite tubulin kinase corresponded to a protein kinase CK2info:eu-repo/semantics/openAccessSociedad de Biología de ChileBiological Research v.36 n.3-4 20032003-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602003000300008en10.4067/S0716-97602003000300008
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	microtubules post-translational modification of tubulin protein kinase CK2 protein phosphorylation-dephosphorylation signal transduction Trypanosoma cruzi tubulin
spellingShingle	microtubules post-translational modification of tubulin protein kinase CK2 protein phosphorylation-dephosphorylation signal transduction Trypanosoma cruzi tubulin UZCANGA,GRACIELA GALÁN-CARIDAD,JOSÉ MANUEL SUAREZ,KAREM NORIS BUBIS,JOSÉ Divalent cation hinder the solubilization of a tubulin kinase activity from Trypanosoma cruzi epimastigotes
description	Trypanosoma cruzi epimastigotes were extracted under various conditions in order to examine the role of divalent cations in the solubilization of microtubule proteins. When epimastigotes were homogenized in the presence of 5 mM Mg+2 and 5 mM Ca+2, a protein kinase responsible for phosphorylating tubulin, as well as the tubulin that became phosphorylated, remained tightly associated with the parasite particulate and detergent-resistant fractions. On the contrary, tubulin kinase and its substrate were predominantly released into the parasite cytosolic and detergent-soluble fractions, when epimastigotes were extracted in the presence of 5 mM EDTA and 5 mM EGTA. These evidences demonstrated a divalent cation-dependent solubilization of the enzyme responsible for the phosphorylation of tubulin in T. cruzi epimastigotes and suggested a tight association between tubulin and this kinase. Under all conditions tested, tubulin kinase activity in epimastigote extracts was lower than the addition of the corresponding value in the parasite cytosolic and membranous fractions, suggesting the presence of a kinase inhibitor or regulatory subunit which also seemed to be modulated by divalent cations. Additionally, inhibition experiments in the presence of heparin, 2,3-bisphosphoglycerate and GTP established that the parasite tubulin kinase corresponded to a protein kinase CK2
author	UZCANGA,GRACIELA GALÁN-CARIDAD,JOSÉ MANUEL SUAREZ,KAREM NORIS BUBIS,JOSÉ
author_facet	UZCANGA,GRACIELA GALÁN-CARIDAD,JOSÉ MANUEL SUAREZ,KAREM NORIS BUBIS,JOSÉ
author_sort	UZCANGA,GRACIELA
title	Divalent cation hinder the solubilization of a tubulin kinase activity from Trypanosoma cruzi epimastigotes
title_short	Divalent cation hinder the solubilization of a tubulin kinase activity from Trypanosoma cruzi epimastigotes
title_full	Divalent cation hinder the solubilization of a tubulin kinase activity from Trypanosoma cruzi epimastigotes
title_fullStr	Divalent cation hinder the solubilization of a tubulin kinase activity from Trypanosoma cruzi epimastigotes
title_full_unstemmed	Divalent cation hinder the solubilization of a tubulin kinase activity from Trypanosoma cruzi epimastigotes
title_sort	divalent cation hinder the solubilization of a tubulin kinase activity from trypanosoma cruzi epimastigotes
publisher	Sociedad de Biología de Chile
publishDate	2003
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602003000300008
work_keys_str_mv	AT uzcangagraciela divalentcationhinderthesolubilizationofatubulinkinaseactivityfromtrypanosomacruziepimastigotes AT galancaridadjosemanuel divalentcationhinderthesolubilizationofatubulinkinaseactivityfromtrypanosomacruziepimastigotes AT suarezkaremnoris divalentcationhinderthesolubilizationofatubulinkinaseactivityfromtrypanosomacruziepimastigotes AT bubisjose divalentcationhinderthesolubilizationofatubulinkinaseactivityfromtrypanosomacruziepimastigotes
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Divalent cation hinder the solubilization of a tubulin kinase activity from Trypanosoma cruzi epimastigotes

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