Calmodulin-binding proteins in the model organism Dictyostelium: A complete &amp; critical review

Catalano, Andrew; O’Day, Danton H.

doi:10.1016/j.cellsig.2007.08.017

Cited by 32 publications

(44 citation statements)

References 206 publications

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“…Calmodulin is a Ca 2+ binding protein that has been proposed to participate in motility in several cell models (Catalano and O'Day, 2008). Because of its apical distribution in Toxoplasma, calmodulin has been suggested to have a role in conoid extrusion (Pezzella-D' Alessandro et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

“…The regulatory protein, calmodulin, is a Ca 2+ sensor protein that presents conformational changes in response to Ca 2+ binding, forming a Ca 2+ -calmodulin complex that stimulates a wide range of enzymes, pumps and other target proteins (Catalano and O'Day, 2008) In Toxoplasma, calmodulin has been reported to be located at the apical end of tachyzoites (Pezzella-D' Alessandro et al, 2001). To examine the role of calmodulin in the conoid extrusion induced by ethanol, two calmodulin antagonists were used (trifluoperazine and calmidazolium).…”

Section: Calmodulin Did Not Participate In the Conoid Extrusion Processmentioning

confidence: 99%

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Induction and regulation of conoid extrusion inToxoplasma gondii

Carmen

Mondragón

González

et al. 2009

Cellular Microbiology

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SummaryCell invasion by the intracellular parasite Toxoplasma gondii occurs through an active process that involves dynamic events, such as gliding motility and conoid extrusion, followed by a sequential secretion from specialized secretory organelles. Increase of intracellular Ca2+ by ionophores induces conoid extrusion, although in an irreversible way, thus limiting the characterization of the regulatory pathways. In this report we studied the effect of different activating conoid conditions to characterize the regulatory mechanisms involved. Exposure of tachyzoites to ethanol, a well-known activator of microneme secretion through the increase of intracellular Ca 2+, induced conoid extrusion without affecting parasite viability nor its in vitro invasive capability, in a process that could be completely reverted and repeatedly reactivated. A temporal relationship between conoid extrusion and microneme secretion was here studied. Under this condition, signal transduction pathways and the precise role of the parasite cytoskeleton were characterized. Our results indicate that phospholipase C, Ca 2+ released through channels sensitive to inositol-3-phosphate and ryanodine, as well as myosin together with actin filaments, but not microtubules, all participate in conoid extrusion. Specific inhibitors for serine-threonine kinases blocked conoid extrusion; in contrast, calmodulin inhibitors did not affect the induction. A regulatory model for conoid activation is here proposed.

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Section: Discussionmentioning

confidence: 99%

Section: Calmodulin Did Not Participate In the Conoid Extrusion Processmentioning

confidence: 99%

Induction and regulation of conoid extrusion inToxoplasma gondii

Carmen

Mondragón

González

et al. 2009

Cellular Microbiology

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“…CaM works in a calcium-dependent or -independent manner by binding to and regulating the activity of target proteins called CaM-binding proteins (CaMBPs), through which Ca 2+ sensitivity is expressed in a variety of cellular regulatory activities (Catalano and O'Day 2008). Our previous results show that the localization of CaM is controlled in a spatio-temporally specific manner (Li et al 1999;Yu et al 2004;Shen et al 2007;Yuan et al 2008), indicating that specific CaM-binding proteins may also function the same way.…”

Section: Discussionmentioning

confidence: 99%

“…CaM-binding proteins (CaMBPs) comprise a diverse group of proteins related solely by the fact that they interact with CaM (Rhoads and Friedberg 1997;O'Day 2003). At present, many CaM-binding proteins have been identified, including protein kinases and phosphatases, proteins involved in second-messenger generation, and proteins that regulate cytoskeletal elements (Selvin 1995;Catalano and O'Day 2008). However, the cell-cycle-related CaM-binding targets are still little known to us, especially their function during cell-cycle checkpoint transition.…”

Section: Introductionmentioning

confidence: 99%

The association of CaM and Hsp70 regulates S-phase arrest and apoptosis in a spatially and temporally dependent manner in human cells

Huang

Wei

Peng

et al. 2009

Cell Stress and Chaperones

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The cell cycle is controlled by regulators functioning at the right time and at the right place. We have found that calmodulin (CaM) has specific distribution patterns during different cell-cycle stages. Here, we identify cell-cycle-specific binding proteins of CaM and examine their function during cell-cycle progression. We first applied immunoprecipitation methods to isolate CaMbinding proteins from cell lysates obtained at different cell-cycle phases and then identified these proteins using mass spectrometry methods. A total of 41 proteins were identified including zinc finger proteins, ribosomal proteins, and heat shock proteins operating in a Ca 2+ -dependent or independent manner. Fifteen proteins were shown to interact with CaM in a cell-phase-specific manner. The association of the selected proteins and CaM were confirmed with in vitro immunoprecipitation and immunostaining methods. One of the identified proteins, heat shock protein 70 (Hsp70), was further studied with respect to its cell-cycle-related function. In vivo fluorescence resonance energy transfer (FRET) analysis showed that the interaction of CaM and Hsp70 was found in the nucleus during the S phase. Overexpression of Hsp70 is shown to arrest cells at S phase and, thus, induce cell apoptosis. When we disrupted the CaM-Hsp70 association with HSP70 truncation without the CaM-binding domain, we found that S-phase arrest and apoptosis could be rescued. The results suggest that the spatial and temporal association of CaM and Hsp70 can regulate cell-cycle progression and cell apoptosis.

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“…It has been hypothesized that myosin II, which localizes in the posterior cell cortex (4,11,32,43,49,81), provides the contractile force for anterior translocation of the cell body and uropod (4,7,23,33,44,65,70,82). For myosin II to localize to the cortex of D. discoideum, it must polymerize, and to polymerize, the myosin II heavy chain (MhcA) must undergo dephosphorylation (13,18,19,37,42,43).…”

Section: Vol 8 2009 How a Cell Crawls 1385mentioning

confidence: 99%

How a Cell Crawls and the Role of Cortical Myosin II

et al. 2009

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The movements of Dictyostelium discoideum amoebae translocating on a glass surface in the absence of chemoattractant have been reconstructed at 5-second intervals and motion analyzed by employing 3D-DIAS software. A morphometric analysis of pseudopods, the main cell body, and the uropod provides a comprehensive description of the basic motile behavior of a cell in four dimensions (4D), resulting in a list of 18 characteristics. A similar analysis of the myosin II phosphorylation mutant 3XASP reveals a role for the cortical localization of myosin II in the suppression of lateral pseudopods, formation of the uropod, cytoplasmic distribution of cytoplasm in the main cell body, and efficient motility. The results of the morphometric analysis suggest that pseudopods, the main cell body, and the uropod represent three motility compartments that are coordinated for efficient translocation. It provides a contextual framework for interpreting the effects of mutations, inhibitors, and chemoattractants on the basic motile behavior of D. discoideum. The generality of the characteristics of the basic motile behavior of D. discoideum must now be tested by similar 4D analyses of the motility of amoeboid cells of higher eukaryotic cells, in particular human polymorphonuclear leukocytes.Amoeboid behavior is a characteristic of cells spanning the entire animal kingdom (5,6,15,56). It is basic to the life history of soil amoebae, embryogenesis, white blood cell function, tissue regeneration, neural development, and cancer metastasis (52). Therefore, the molecular biology of this process has been the focus of intensive investigation (2,15,40,50,53,57). In marked contrast, the basic motile behavior of amoeboid cells, which provides the contextual framework for interpreting the results of genetic and biochemical studies, has received far less attention. We still lack an accurate and quantitative fourdimensional (4D) description of how an amoeboid cell translocates along a substratum in the absence of a chemotactic signal. The lack of such a description has led to perceptions of single cell migration that are 2D, sometimes oversimplified, and sometimes actually inaccurate. These perceptions, unfortunately, have served as the basis for modeling cell locomotion, interpreting the behavioral defects of cytoskeletal and regulatory mutants, and assessing the effects of inhibitors and stimuli, most notably chemoattractants.To obtain a 4D description of cell behavior, we have employed 3D-DIAS software (25,61,62,64,78) to reconstruct and motion analyze the basic motile behavior of Dictyostelium discoideum amoebae translocating along a substratum in the absence of chemoattractant (63,71,76,77,79,80). By quantitating in space and time the extension and retraction of pseudopods, changes in shape, anterior progress of the main cell body and uropod, and contact of the ventral surface of the cell with the substratum, we have developed a complex morphometric description of cell migration that reveals a number of characteristics. In addition, by simil...

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Calmodulin-binding proteins in the model organism Dictyostelium: A complete & critical review

Cited by 32 publications

References 206 publications

Induction and regulation of conoid extrusion inToxoplasma gondii

Induction and regulation of conoid extrusion inToxoplasma gondii

The association of CaM and Hsp70 regulates S-phase arrest and apoptosis in a spatially and temporally dependent manner in human cells

How a Cell Crawls and the Role of Cortical Myosin II

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