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  1. Article ; Online: A divergent calponin homology (NN-CH) domain defines a novel family: implications for evolution of ciliary IFT complex B proteins.

    Schou, Kenneth B / Andersen, Jens S / Pedersen, Lotte B

    Bioinformatics (Oxford, England)

    2013  Volume 30, Issue 7, Page(s) 899–902

    Abstract: Motivation: Microtubules are dynamic polymers of tubulin dimers that undergo continuous assembly and disassembly. A mounting number of microtubule-associated proteins (MAPs) regulate the dynamic behavior of microtubules and hence the assembly and ... ...

    Abstract Motivation: Microtubules are dynamic polymers of tubulin dimers that undergo continuous assembly and disassembly. A mounting number of microtubule-associated proteins (MAPs) regulate the dynamic behavior of microtubules and hence the assembly and disassembly of disparate microtubule structures within the cell. Despite recent advances in identification and functional characterization of MAPs, a substantial number of microtubule accessory factors have not been functionally annotated. Here, using profile-to-profile comparisons and structure modeling, we show that the yeast outer kinetochore components NDC80 and NUF2 share evolutionary ancestry with a novel protein family in mammals comprising, besides NDC80/HEC1 and NUF2, three Intraflagellar Transport (IFT) complex B subunits (IFT81, IFT57, CLUAP1) as well as six proteins with poorly defined function (FAM98A-C, CCDC22, CCDC93 and C14orf166). We show that these proteins consist of a divergent N-terminal calponin homology (CH)-like domain adjoined to an array of C-terminal heptad repeats predicted to form a coiled-coil arrangement. We have named the divergent CH-like domain NN-CH after the founding members NDC80 and NUF2.
    MeSH term(s) Amino Acid Sequence ; Animals ; Calcium-Binding Proteins/chemistry ; Calcium-Binding Proteins/genetics ; Calcium-Binding Proteins/metabolism ; Evolution, Molecular ; Humans ; Kinetochores/metabolism ; Microfilament Proteins/chemistry ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Molecular Sequence Data ; Nuclear Proteins/chemistry ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Protein Binding ; Saccharomyces cerevisiae/chemistry ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Sequence Alignment ; Sequence Analysis, Protein ; Calponins
    Chemical Substances Calcium-Binding Proteins ; Microfilament Proteins ; Nuclear Proteins
    Language English
    Publishing date 2013-11-20
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1422668-6
    ISSN 1367-4811 ; 1367-4803
    ISSN (online) 1367-4811
    ISSN 1367-4803
    DOI 10.1093/bioinformatics/btt661
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2374: Show issues Location:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  2. Article: Identification of conserved, centrosome-targeting ASH domains in TRAPPII complex subunits and TRAPPC8.

    Schou, Kenneth B / Morthorst, Stine K / Christensen, Søren T / Pedersen, Lotte B

    Cilia

    2014  Volume 3, Page(s) 6

    Abstract: Background: Assembly of primary cilia relies on vesicular trafficking towards the cilium base and intraflagellar transport (IFT) between the base and distal tip of the cilium. Recent studies have identified several key regulators of these processes, ... ...

    Abstract Background: Assembly of primary cilia relies on vesicular trafficking towards the cilium base and intraflagellar transport (IFT) between the base and distal tip of the cilium. Recent studies have identified several key regulators of these processes, including Rab GTPases such as Rab8 and Rab11, the Rab8 guanine nucleotide exchange factor Rabin8, and the transport protein particle (TRAPP) components TRAPPC3, -C9, and -C10, which physically interact with each other and function together with Bardet Biedl syndrome (BBS) proteins in ciliary membrane biogenesis. However, despite recent advances, the exact molecular mechanisms by which these proteins interact and target to the basal body to promote ciliogenesis are not fully understood.
    Results: We surveyed the human proteome for novel ASPM, SPD-2, Hydin (ASH) domain-containing proteins. We identified the TRAPP complex subunits TRAPPC8, -9, -10, -11, and -13 as novel ASH domain-containing proteins. In addition to a C-terminal ASH domain region, we predict that the N-terminus of TRAPPC8, -9, -10, and -11, as well as their yeast counterparts, consists of an α-solenoid bearing stretches of multiple tetratricopeptide (TPR) repeats. Immunofluorescence microscopy analysis of cultured mammalian cells revealed that exogenously expressed ASH domains, as well as endogenous TRAPPC8, localize to the centrosome/basal body. Further, depletion of TRAPPC8 impaired ciliogenesis and GFP-Rabin8 centrosome targeting.
    Conclusions: Our results suggest that ASH domains confer targeting to the centrosome and cilia, and that TRAPPC8 has cilia-related functions. Further, we propose that the yeast TRAPPII complex and its mammalian counterpart are evolutionarily related to the bacterial periplasmic trafficking chaperone PapD of the usher pili assembly machinery.
    Language English
    Publishing date 2014-06-18
    Publishing country England
    Document type Journal Article
    ZDB-ID 2689513-4
    ISSN 2046-2530
    ISSN 2046-2530
    DOI 10.1186/2046-2530-3-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Human RTEL1 associates with Poldip3 to facilitate responses to replication stress and R-loop resolution.

    Björkman, Andrea / Johansen, Søren L / Lin, Lin / Schertzer, Mike / Kanellis, Dimitris C / Katsori, Anna-Maria / Christensen, Søren T / Luo, Yonglun / Andersen, Jens S / Elsässer, Simon J / Londono-Vallejo, Arturo / Bartek, Jiri / Schou, Kenneth B

    Genes & development

    2020  Volume 34, Issue 15-16, Page(s) 1065–1074

    Abstract: RTEL1 helicase is a component of DNA repair and telomere maintenance machineries. While RTEL1's role in DNA replication is emerging, how RTEL1 preserves genomic stability during replication remains elusive. Here we used a range of proteomic, biochemical, ...

    Abstract RTEL1 helicase is a component of DNA repair and telomere maintenance machineries. While RTEL1's role in DNA replication is emerging, how RTEL1 preserves genomic stability during replication remains elusive. Here we used a range of proteomic, biochemical, cell, and molecular biology and gene editing approaches to provide further insights into potential role(s) of RTEL1 in DNA replication and genome integrity maintenance. Our results from complementary human cell culture models established that RTEL1 and the Polδ subunit Poldip3 form a complex and are/function mutually dependent in chromatin binding after replication stress. Loss of RTEL1 and Poldip3 leads to marked R-loop accumulation that is confined to sites of active replication, enhances endogenous replication stress, and fuels ensuing genomic instability. The impact of depleting RTEL1 and Poldip3 is epistatic, consistent with our proposed concept of these two proteins operating in a shared pathway involved in DNA replication control under stress conditions. Overall, our data highlight a previously unsuspected role of RTEL1 and Poldip3 in R-loop suppression at genomic regions where transcription and replication intersect, with implications for human diseases including cancer.
    MeSH term(s) Cell Line ; Chromatin/metabolism ; DNA Helicases/metabolism ; DNA Replication ; Humans ; R-Loop Structures ; RNA-Binding Proteins/metabolism ; Stress, Physiological ; Topoisomerase I Inhibitors/pharmacology
    Chemical Substances Chromatin ; POLDIP3 protein, human ; RNA-Binding Proteins ; Topoisomerase I Inhibitors ; RTEL1 protein, human (EC 3.6.1.-) ; DNA Helicases (EC 3.6.4.-)
    Language English
    Publishing date 2020-06-19
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 806684-x
    ISSN 1549-5477 ; 0890-9369
    ISSN (online) 1549-5477
    ISSN 0890-9369
    DOI 10.1101/gad.330050.119
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2292: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 54: Show issues

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  4. Article ; Online: KIF13B establishes a CAV1-enriched microdomain at the ciliary transition zone to promote Sonic hedgehog signalling.

    Schou, Kenneth B / Mogensen, Johanne B / Morthorst, Stine K / Nielsen, Brian S / Aleliunaite, Aiste / Serra-Marques, Andrea / Fürstenberg, Nicoline / Saunier, Sophie / Bizet, Albane A / Veland, Iben R / Akhmanova, Anna / Christensen, Søren T / Pedersen, Lotte B

    Nature communications

    2017  Volume 8, Page(s) 14177

    Abstract: Ciliary membrane composition is controlled by transition zone (TZ) proteins such as RPGRIP1, RPGRIPL and NPHP4, which are vital for balanced coordination of diverse signalling systems like the Sonic hedgehog (Shh) pathway. Activation of this pathway ... ...

    Abstract Ciliary membrane composition is controlled by transition zone (TZ) proteins such as RPGRIP1, RPGRIPL and NPHP4, which are vital for balanced coordination of diverse signalling systems like the Sonic hedgehog (Shh) pathway. Activation of this pathway involves Shh-induced ciliary accumulation of Smoothened (SMO), which is disrupted by disease-causing mutations in TZ components. Here we identify kinesin-3 motor protein KIF13B as a novel member of the RPGRIP1N-C2 domain-containing protein family and show that KIF13B regulates TZ membrane composition and ciliary SMO accumulation. KIF13B is upregulated during ciliogenesis and is recruited to the ciliary base by NPHP4, which binds to two distinct sites in the KIF13B tail region, including an RPGRIP1N-C2 domain. KIF13B and NPHP4 are both essential for establishment of a CAV1 membrane microdomain at the TZ, which in turn is required for Shh-induced ciliary SMO accumulation. Thus KIF13B is a novel regulator of ciliary TZ configuration, membrane composition and Shh signalling.
    MeSH term(s) Animals ; Caveolin 1/metabolism ; Cell Line ; Cell Membrane/metabolism ; Cell Membrane/physiology ; Cilia/physiology ; Computational Biology ; Gene Expression Profiling ; Gene Expression Regulation/physiology ; Gene Knockout Techniques ; HEK293 Cells ; Hedgehog Proteins/metabolism ; Humans ; Kinesin/genetics ; Kinesin/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; NIH 3T3 Cells ; Protein Domains/physiology ; Proteins/metabolism ; Signal Transduction/physiology ; Smoothened Receptor/metabolism ; Up-Regulation ; Zinc Finger Protein GLI1/genetics ; Zinc Finger Protein GLI1/metabolism
    Chemical Substances CAV1 protein, human ; Caveolin 1 ; GLI1 protein, human ; Hedgehog Proteins ; Membrane Proteins ; NPHP4 protein, human ; NPHP4 protein, mouse ; Proteins ; SHH protein, human ; SMO protein, human ; Smoothened Receptor ; Zinc Finger Protein GLI1 ; KIF13B protein, human (EC 3.6.1.-) ; KIF13b protein, mouse (EC 3.6.1.-) ; Kinesin (EC 3.6.4.4)
    Language English
    Publishing date 2017-01-30
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2041-1723
    ISSN (online) 2041-1723
    DOI 10.1038/ncomms14177
    Database MEDical Literature Analysis and Retrieval System OnLINE

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