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  1. Article ; Online: Updates on ion and water transport by the Malpighian tubule.

    Dow, Julian A T / Krause, Sue Ann / Herzyk, Pawel

    Current opinion in insect science

    2021  Volume 47, Page(s) 31–37

    Abstract: The Malpighian (renal) tubule is capable of transporting fluid at remarkable rates. This review will focus on recent insights into the mechanisms by which these high rates are achieved and controlled, with particular reference to the tubules of ... ...

    Abstract The Malpighian (renal) tubule is capable of transporting fluid at remarkable rates. This review will focus on recent insights into the mechanisms by which these high rates are achieved and controlled, with particular reference to the tubules of Drosophila melanogaster, in which the combination of physiology and genetics has led to particularly rapid progress. Like many vertebrate epithelia, the Drosophila tubule has specialized cell types, with active cation transport confined to a large, metabolically active principal cell; whereas the smaller intercalated stellate cell controls chloride and water shunts to achieve net fluid secretion. Recently, the genes underlying many of these processes have been identified, functionally validated and localized within the tubule. The imminent arrival of new types of post-genomic data (notably single cell sequencing) will herald an exciting era of new discovery.
    MeSH term(s) Animals ; Drosophila Proteins/metabolism ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Ion Transport ; Malpighian Tubules ; Water/metabolism
    Chemical Substances Drosophila Proteins ; Water (059QF0KO0R)
    Language English
    Publishing date 2021-03-08
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2772833-X
    ISSN 2214-5753 ; 2214-5745
    ISSN (online) 2214-5753
    ISSN 2214-5745
    DOI 10.1016/j.cois.2021.02.018
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Updates on ion and water transport by the Malpighian tubule

    Dow, Julian A T / Krause, Sue Ann / Herzyk, Pawel

    Current Opinion in Insect Science. 2021 Oct., v. 47 p.31-37

    2021  

    Abstract: The Malpighian (renal) tubule is capable of transporting fluid at remarkable rates. This review will focus on recent insights into the mechanisms by which these high rates are achieved and controlled, with particular reference to the tubules of ... ...

    Abstract The Malpighian (renal) tubule is capable of transporting fluid at remarkable rates. This review will focus on recent insights into the mechanisms by which these high rates are achieved and controlled, with particular reference to the tubules of Drosophila melanogaster, in which the combination of physiology and genetics has led to particularly rapid progress. Like many vertebrate epithelia, the Drosophila tubule has specialized cell types, with active cation transport confined to a large, metabolically active principal cell; whereas the smaller intercalated stellate cell controls chloride and water shunts to achieve net fluid secretion. Recently, the genes underlying many of these processes have been identified, functionally validated and localized within the tubule. The imminent arrival of new types of post-genomic data (notably single cell sequencing) will herald an exciting era of new discovery.
    Keywords Drosophila melanogaster ; Malpighian tubules ; cations ; chlorides ; genetics ; insects ; secretion ; vertebrates
    Language English
    Dates of publication 2021-10
    Size p. 31-37.
    Publishing place Elsevier Inc.
    Document type Article ; Online
    Note Use and reproduction
    ZDB-ID 2772833-X
    ISSN 2214-5753 ; 2214-5745
    ISSN (online) 2214-5753
    ISSN 2214-5745
    DOI 10.1016/j.cois.2021.02.018
    Database NAL-Catalogue (AGRICOLA)

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  3. Article: The protein kinase C pathway is required for viability in quiescence in Saccharomyces cerevisiae.

    Krause, Sue Ann / Gray, Joseph V

    Current biology : CB

    2002  Volume 12, Issue 7, Page(s) 588–593

    Abstract: Protein kinase C, encoded by PKC1, regulates construction of the cell surface in vegetatively growing yeast cells. Pkc1 in part acts by regulating Mpk1, a MAP kinase. Mutants lacking Bck1, a component of the MAP kinase branch of the pathway, fail to ... ...

    Abstract Protein kinase C, encoded by PKC1, regulates construction of the cell surface in vegetatively growing yeast cells. Pkc1 in part acts by regulating Mpk1, a MAP kinase. Mutants lacking Bck1, a component of the MAP kinase branch of the pathway, fail to respond normally to nitrogen starvation, which causes entry into quiescence. Given that the Tor1 and Tor2 proteins are key inhibitors of entry into quiescence, the Pkc1 pathway may regulate these proteins. We find that pkc1Delta and mpk1Delta mutants rapidly die by cell lysis upon carbon or nitrogen starvation. The Pkc1 pathway does not regulate the TOR proteins: transcriptional changes dependent on inhibition of the TORs occur normally in pkc1Delta and mpk1Delta mutants when starved for nitrogen; pkc1Delta and mpk1Delta mutants die rapidly upon treatment with rapamycin, an inhibitor of the TORs. We find that Mpk1 is transiently activated by rapamycin treatment via a novel mechanism. Finally, we find that rapamycin treatment or nitrogen starvation induces resistance to the cell wall-digesting enzyme zymolyase by a Pkc1-dependent mechanism. Thus, the Pkc1 pathway is not a nutrient sensor but acts downstream of TOR inhibition to maintain cell integrity in quiescence.
    MeSH term(s) Amino Acid Transport Systems ; Carrier Proteins/metabolism ; Cation Transport Proteins ; Cell Cycle Proteins ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Membrane Proteins/metabolism ; Mitogen-Activated Protein Kinase Kinases ; Mitogen-Activated Protein Kinases/metabolism ; Mutagenesis ; Phosphatidylinositol 3-Kinases ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Protein Kinase C/genetics ; Protein Kinase C/metabolism ; Protein Kinases/genetics ; Protein Kinases/metabolism ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae Proteins ; Signal Transduction ; ras GTPase-Activating Proteins/metabolism
    Chemical Substances Amino Acid Transport Systems ; Carrier Proteins ; Cation Transport Proteins ; Cell Cycle Proteins ; Fungal Proteins ; GAP1 protein, S cerevisiae ; MEP2 protein, S cerevisiae ; Membrane Proteins ; SLG1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; ras GTPase-Activating Proteins ; Protein Kinases (EC 2.7.-) ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Phosphotransferases (Alcohol Group Acceptor) (EC 2.7.1.-) ; TOR1 protein, S cerevisiae (EC 2.7.1.137) ; TOR2 protein, S cerevisiae (EC 2.7.1.137) ; BCK1 protein, S cerevisiae (EC 2.7.11.1) ; Protein Kinase C (EC 2.7.11.13) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; SLT2 protein, S cerevisiae (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase Kinases (EC 2.7.12.2)
    Language English
    Publishing date 2002-04-02
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/s0960-9822(02)00760-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3208: Show issues Location:
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  4. Article ; Online: Functional specialisation of yeast Rho1 GTP exchange factors.

    Krause, Sue Ann / Cundell, Michael J / Poon, Pak P / McGhie, Josephine / Johnston, Gerry C / Price, Clive / Gray, Joseph V

    Journal of cell science

    2012  Volume 125, Issue Pt 11, Page(s) 2721–2731

    Abstract: Rho GTPases are regulated in complex spatiotemporal patterns that might be dependent, in part at least, on the multiplicity of their GTP exchange factors (GEFs). Here, we examine the extent of and basis for functional specialisation of the Rom2 and Tus1 ... ...

    Abstract Rho GTPases are regulated in complex spatiotemporal patterns that might be dependent, in part at least, on the multiplicity of their GTP exchange factors (GEFs). Here, we examine the extent of and basis for functional specialisation of the Rom2 and Tus1 GEFs that activate the yeast Rho1 GTPase, the orthologue of mammalian RhoA. First, we find that these GEFs selectively activate different Rho1-effector branches. Second, the synthetic genetic networks around ROM2 and TUS1 confirm very different global in vivo roles for these GEFs. Third, the GEFs are not functionally interchangeable: Tus1 cannot replace the essential role of Rom2, even when overexpressed. Fourth, we find that Rom2 and Tus1 localise differently: Rom2 to the growing bud surface and to the bud neck at cytokinesis; Tus1 only to the bud neck, but in a distinct pattern. Finally, we find that these GEFs are dependent on different protein co-factors: Rom2 function and localisation is largely dependent on Ack1, a SEL1-domain-containing protein; Tus1 function and localisation is largely dependent on the Tus1-interacting protein Ypl066w (which we name Rgl1). We have revealed a surprising level of diversity among the Rho1 GEFs that contributes another level of complexity to the spatiotemporal control of Rho1.
    MeSH term(s) Gene Regulatory Networks/genetics ; Guanine Nucleotide Exchange Factors/metabolism ; Guanosine Triphosphate/metabolism ; Mutation/genetics ; Protein Transport ; Saccharomyces cerevisiae/cytology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction ; Time Factors ; rho GTP-Binding Proteins/metabolism
    Chemical Substances Guanine Nucleotide Exchange Factors ; ROM2 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; TUS1 protein, S cerevisiae ; Guanosine Triphosphate (86-01-1) ; RHO1 protein, S cerevisiae (EC 3.6.5.2) ; rho GTP-Binding Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2012-06-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.100685
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1200: Show issues Location:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
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    Zs.MG 14: Show issues

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  5. Article: Mpt5p, a stress tolerance- and lifespan-promoting PUF protein in Saccharomyces cerevisiae, acts upstream of the cell wall integrity pathway.

    Stewart, Mark S / Krause, Sue Ann / McGhie, Josephine / Gray, Joseph V

    Eukaryotic cell

    2006  Volume 6, Issue 2, Page(s) 262–270

    Abstract: Pumilio family (PUF) proteins affect specific genes by binding to, and inhibiting the translation or stability of, their transcripts. The PUF domain is required and sufficient for this function. One Saccharomyces cerevisiae PUF protein, Mpt5p (also ... ...

    Abstract Pumilio family (PUF) proteins affect specific genes by binding to, and inhibiting the translation or stability of, their transcripts. The PUF domain is required and sufficient for this function. One Saccharomyces cerevisiae PUF protein, Mpt5p (also called Puf5p or Uth4p), promotes stress tolerance and replicative life span (the maximum number of doublings a mother cell can undergo before entering into senescence) by an unknown mechanism thought to partly overlap with, but to be independent of, the cell wall integrity (CWI) pathway. Here, we found that mpt5Delta mutants also display a short chronological life span (the time cells stay alive in saturated cultures in synthetic medium), a defect that is suppressed by activation of CWI signaling. We found that Mpt5p is an upstream activator of the CWI pathway: mpt5Delta mutants display the appropriate phenotypes and genetic interactions, display low basal activity of the pathway, and are defective in activation of the pathway upon thermal stress. A set of mRNAs that specifically bind to Mpt5p was recently reported. One such putative target, LRG1, encodes a GTPase-activating protein for Rho1p that directly links Mpt5p to CWI signaling: Lrg1p inhibits CWI signaling, LRG1 mRNA contains a consensus Mpt5p-binding site in its putative 3' untranslated region, loss of Lrg1p suppresses the temperature sensitivity and CWI signaling defects of mpt5Delta mutants, and LRG1 mRNA abundance is inhibited by Mpt5p. We conclude that Mpt5p is required for normal replicative and chronological life spans and that the CWI pathway is a key and direct downstream target of this PUF protein.
    MeSH term(s) Adaptation, Physiological ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cell Survival ; Cell Wall/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; GTPase-Activating Proteins ; Gene Expression Regulation, Fungal ; Longevity/physiology ; RNA-Binding Proteins ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction
    Chemical Substances Cell Cycle Proteins ; DNA-Binding Proteins ; GTPase-Activating Proteins ; LRG1 protein, S cerevisiae ; MPT5 protein, S cerevisiae ; RNA-Binding Proteins ; Repressor Proteins ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2006-12-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2077635-4
    ISSN 1535-9786 ; 1535-9778
    ISSN (online) 1535-9786
    ISSN 1535-9778
    DOI 10.1128/EC.00188-06
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 5779: Show issues Location:
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