TcSCA Complements Yeast Mutants Defective in Ca2+ Pumps and Encodes a Ca2+-ATPase That Localizes to the Endoplasmic Reticulum of Trypanosoma cruzi

Furuya, Tetsuya; Okura, Michael; Ruiz, Félix A.; Scott, David A.; Docampo, Roberto

doi:10.1074/jbc.m104000200

Cited by 40 publications

(38 citation statements)

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“…The rapid and robust increase in giardial [Ca 2ϩ ] i in response to TG suggests that this storage system may have a large capacity to store Ca 2ϩ and that the Ca 2ϩ cycles into and out of the storage compartment rapidly. Thus, kinetically, the TG-sensitive Ca 2ϩ storage compartment in Giardia resembles the SERCA pump-leak system found in many mammalian cells (18,36). The ability of G. lamblia to release Ca 2ϩ into the cytoplasm in response to TG was evident throughout the life cycle.…”

Section: And This Work)mentioning

confidence: 86%

“…Ca 2ϩ is also sequestered within internal storage compartments, mainly the endoplasmic reticulum (ER) 1 (16 -19). Later diverging eukaryotes (17,18) have one or more Ca 2ϩ -ATPases (sarcoplasmic/endoplasmic reticulum calcium ATPase, SERCA), pumps that maintain low cytosolic Ca 2ϩ by pumping it into a membrane compartment, generally the ER in non-muscle cells and the SR in muscle cells. This pump also retrieves Ca 2ϩ that has leaked into the cytosol and is critical for Ca 2ϩ homeostasis and cell function (17).…”

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confidence: 99%

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Calcium Signaling in Excystation of the Early Diverging Eukaryote, Giardia lamblia

Reiner

Hetsko

Meszaros

et al. 2003

Journal of Biological Chemistry

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Excystation of Giardia lamblia, which initiates infection, is a poorly understood but dramatic differentiation induced by physiological signals from the host. Our data implicate a central role for calcium homeostasis in excystation. Agents that alter cytosolic Ca 2؉ levels (1,2-bis(2-aminophenoxy)ethane-N,N,N ,N -tetraacetic acidtetra(acetyloxymethyl) ester, a Ca 2؉ channel blocker, Ca 2؉ ionophores, and thapsigargin) strongly inhibit excystation. Treatment of Giardia with thapsigargin raised intracellular Ca 2؉ levels, and peak Ca 2؉ responses increased with each stage of excystation, consistent with the kinetics of inhibition. Fluorescent thapsigargin localized to a likely Ca 2؉ storage compartment in cysts. The ability to sequester ions in membranebounded compartments is a hallmark of the eukaryotic cell. These studies support the existence of a giardial thapsigargin-sensitive Ca 2؉ storage compartment resembling the sarcoplasmic/endoplasmic reticulum calcium ATPase pump-leak system and suggest that it is important in regulation of differentiation and appeared early in the evolution of eukaryotic cells. Calmodulin antagonists also blocked excystation. The divergent giardial calmodulin localized to the eight flagellar basal bodies/centrosomes, like protein kinase A. Inhibitor kinetics suggest that protein kinase A signaling triggers excystation, whereas calcium signaling is mainly required later, for parasite activation and emergence.

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Section: And This Work)mentioning

confidence: 86%

mentioning

confidence: 99%

Calcium Signaling in Excystation of the Early Diverging Eukaryote, Giardia lamblia

Reiner

Hetsko

Meszaros

et al. 2003

Journal of Biological Chemistry

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“…4 panel C). The anti-BiP antibody used in this experiment is specific to T. brucei and was shown to localize the BiP protein in the endoplasmic reticulum of this parasite (35), as well as in the related trypanosomatid parasites Trypanosoma cruzi (36) and Leishmania mexicana amazonensis (37). No fluorescence was seen in promastigotes treated with a normal rabbit serum (Fig.…”

Section: Resultsmentioning

confidence: 99%

An Atypical Protein Disulfide Isomerase from the Protozoan Parasite Leishmania Containing a Single Thioredoxin-like Domain

Alejandro¹,

Noiva

Lee³

et al. 2003

Journal of Biological Chemistry

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In higher eukaryotes, secretory proteins are under the quality control of the endoplasmic reticulum for their proper folding and release into the secretory pathway. One of the proteins involved in the quality control is protein disulfide isomerase, which catalyzes the formation of protein disulfide bonds. As a first step toward understanding the endoplasmic reticulum quality control of secretory proteins in lower eukaryotes, we have isolated a protein disulfide isomerase gene from the protozoan parasite Leishmania donovani. The parasite enzyme shows high sequence homology with homologs from other organisms. However, unlike the four thioredoxin-like domains found in most protein disulfide isomerases, of which two contain an active site, the leishmanial enzyme possesses only one active site present in a single thioredoxin-like domain. When expressed in Escherichia coli, the recombinant parasite enzyme shows both oxidase and isomerase activities. Replacement of the two cysteins with alanines in its active site results in loss of both enzymatic activities. Further, overexpression of the mutated/inactive form of the parasite enzyme in L. donovani significantly reduced their release of secretory acid phosphatases, suggesting that this single thioredoxin-like domain protein disulfide isomerase could play a critical role in the Leishmania secretory pathway.

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“…Many PMR1 homologs from other yeasts (40,66,86) were found to complement the S. cerevisiae pmr1 mutant. In addition, newly discovered SERCA-and PMCA-type Ca 2ϩ pumps from diverse organisms also restore wild-type phenotypes in yeast lacking endogenous pumps and have been biochemically characterized (23,31,48,49,78). Heterologous expression of rabbit SERCA1 in yeast has been used to produce protein for biochemical analysis of site-directed mutants (46).…”

Section: Secretory Pathway Ca 2؉ -Atpase Defective In Hailey-hailey Dmentioning

confidence: 99%

“…In laboratories around the world, many types of genes from bacteria (56), protozoa (7,12,31), fungi (100), plants (48), and animals (83) have been expressed in and shown to complement deletion phenotypes of yeast mutants. The references given here are a very few examples of the vast number of articles published on the subject of functional complementation studies in yeast.…”

Section: Heterologous Expression In Yeastmentioning

confidence: 99%

Functional expression of heterologous proteins in yeast: insights into Ca²⁺signaling and Ca²⁺-transporting ATPases

Ton¹,

Rao²

2004

American Journal of Physiology-Cell Physiology

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TcSCA Complements Yeast Mutants Defective in Ca2+ Pumps and Encodes a Ca2+-ATPase That Localizes to the Endoplasmic Reticulum of Trypanosoma cruzi

Abstract: Intracellular Ca2؉ in Trypanosoma cruzi is mainly located in an acidic compartment named the acidocalcisome, which among other pumps and exchangers possesses a plasma membrane-type Ca

Cited by 40 publications

References 60 publications

Calcium Signaling in Excystation of the Early Diverging Eukaryote, Giardia lamblia

Calcium Signaling in Excystation of the Early Diverging Eukaryote, Giardia lamblia

An Atypical Protein Disulfide Isomerase from the Protozoan Parasite Leishmania Containing a Single Thioredoxin-like Domain

Functional expression of heterologous proteins in yeast: insights into Ca²⁺signaling and Ca²⁺-transporting ATPases

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TcSCA Complements Yeast Mutants Defective in Ca2+ Pumps and Encodes a Ca2+-ATPase That Localizes to the Endoplasmic Reticulum of Trypanosoma cruzi

Abstract: Intracellular Ca2؉ in Trypanosoma cruzi is mainly located in an acidic compartment named the acidocalcisome, which among other pumps and exchangers possesses a plasma membrane-type Ca

Cited by 40 publications

References 60 publications

Calcium Signaling in Excystation of the Early Diverging Eukaryote, Giardia lamblia

Calcium Signaling in Excystation of the Early Diverging Eukaryote, Giardia lamblia

An Atypical Protein Disulfide Isomerase from the Protozoan Parasite Leishmania Containing a Single Thioredoxin-like Domain

Functional expression of heterologous proteins in yeast: insights into Ca2+signaling and Ca2+-transporting ATPases

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Product

Resources

About

Functional expression of heterologous proteins in yeast: insights into Ca²⁺signaling and Ca²⁺-transporting ATPases