LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 10 of total 131

Search options

  1. Article ; Online: Development of an expression system in Tetrahymena inner arm dyneins and motile properties of the single-headed subspecies (Dyh8p and Dyh12p).

    Edamatsu, Masaki

    Biochemical and biophysical research communications

    2019  Volume 523, Issue 1, Page(s) 253–257

    Abstract: Diverse inner arm dyneins cooperate with outer arm dyneins to produce ciliary beating. This study demonstrates an expression system for inner arm dyneins in Tetrahymena. The motor domain of inner arm dynein (Dyh8p or Dyh12p) was fused with the tail of ... ...

    Abstract Diverse inner arm dyneins cooperate with outer arm dyneins to produce ciliary beating. This study demonstrates an expression system for inner arm dyneins in Tetrahymena. The motor domain of inner arm dynein (Dyh8p or Dyh12p) was fused with the tail of outer arm dynein (Dyh3p) and expressed in viable DYH3-knockout (vKO-DYH3) cells. The chimeric dyneins were observed in the oral apparatus and cilia on the cell bodies, and did not change the swimming speed of vKO-DYH3 cells. In a gliding assay, the motor domains of Dyh8p and Dyh12p moved toward the minus ends of microtubules at 0.8 and 0.3 μm/s, respectively. The gliding velocities of Dyh8p and Dyh12p were decreased in 5 mM ATP but not increased in 0.1 or 0.5 mM ADP. This expression system will be useful for molecular studies on diverse inner arm dyneins.
    MeSH term(s) Cilia/genetics ; Cilia/metabolism ; Dyneins/genetics ; Dyneins/isolation & purification ; Dyneins/metabolism ; Protein Subunits/genetics ; Protein Subunits/metabolism ; Tetrahymena/cytology ; Tetrahymena/genetics ; Tetrahymena/metabolism
    Chemical Substances Protein Subunits ; Dyneins (EC 3.6.4.2)
    Language English
    Publishing date 2019-12-19
    Publishing country United States
    Document type Journal Article
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2019.12.062
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 116: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article ; Online: Functional characterization of lethal P-loop mutations in Tetrahymena outer arm dynein (Dyh3p).

    Edamatsu, Masaki

    Biochemical and biophysical research communications

    2018  Volume 496, Issue 4, Page(s) 1382–1388

    Abstract: Mutational analyses of axonemal dyneins are useful for elucidating the molecular mechanism of ciliary motility. This study demonstrates a mutation system for characterizing lethal P-loop mutations in Tetrahymena outer arm dynein (Dyh3p). The viable DYH3- ... ...

    Abstract Mutational analyses of axonemal dyneins are useful for elucidating the molecular mechanism of ciliary motility. This study demonstrates a mutation system for characterizing lethal P-loop mutations in Tetrahymena outer arm dynein (Dyh3p). The viable DYH3-knockout (vKO-DYH3) cells isolated in this study enabled the examination of lethal mutations in P-loops 1 and 2. The P1 mutant dynein localized in the oral apparatus and the proximal region of the cilia, and the P2 mutant dynein localized only in the oral apparatus. Both results are different from the localization of wild-type Dyh3p. In addition, a co-precipitation assay showed that the P1 and P2 mutant dyneins did not dissociate from microtubules in ATP plus vanadate or in no-ATP conditions, in contrast to wild-type Dyh3p. This mutation system is useful for further molecular studies of axonemal dyneins and ciliary motility.
    MeSH term(s) AAA Domain/genetics ; Cell Movement/physiology ; Cilia/physiology ; Mutation/genetics ; Protozoan Proteins/genetics ; Structure-Activity Relationship ; Tetrahymena/physiology
    Chemical Substances Protozoan Proteins
    Language English
    Publishing date 2018--19
    Publishing country United States
    Document type Journal Article
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2018.02.038
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 116: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article: Development of an expression system in Tetrahymena inner arm dyneins and motile properties of the single-headed subspecies (Dyh8p and Dyh12p)

    Edamatsu, Masaki

    Biochemical and biophysical research communications. 2020 Feb. 26, v. 523, no. 1

    2020  

    Abstract: Diverse inner arm dyneins cooperate with outer arm dyneins to produce ciliary beating. This study demonstrates an expression system for inner arm dyneins in Tetrahymena. The motor domain of inner arm dynein (Dyh8p or Dyh12p) was fused with the tail of ... ...

    Abstract Diverse inner arm dyneins cooperate with outer arm dyneins to produce ciliary beating. This study demonstrates an expression system for inner arm dyneins in Tetrahymena. The motor domain of inner arm dynein (Dyh8p or Dyh12p) was fused with the tail of outer arm dynein (Dyh3p) and expressed in viable DYH3-knockout (vKO-DYH3) cells. The chimeric dyneins were observed in the oral apparatus and cilia on the cell bodies, and did not change the swimming speed of vKO-DYH3 cells. In a gliding assay, the motor domains of Dyh8p and Dyh12p moved toward the minus ends of microtubules at 0.8 and 0.3 μm/s, respectively. The gliding velocities of Dyh8p and Dyh12p were decreased in 5 mM ATP but not increased in 0.1 or 0.5 mM ADP. This expression system will be useful for molecular studies on diverse inner arm dyneins.
    Keywords Tetrahymena ; dynein ATPase ; microtubules ; research
    Language English
    Dates of publication 2020-0226
    Size p. 253-257.
    Publishing place Elsevier Inc.
    Document type Article
    Note NAL-AP-2-clean
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2019.12.062
    Database NAL-Catalogue (AGRICOLA)

    More links

    Kategorien

    In stock of ZB MED Bonn / Germany

    Z 71/706: Show issues
    Z 3.8: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  4. Article ; Online: Establishment of a mutation system in Tetrahymena outer arm dynein and P-loop functions of the alpha heavy chain (Dyh3p).

    Edamatsu, Masaki

    Biochemical and biophysical research communications

    2017  Volume 483, Issue 1, Page(s) 24–31

    Abstract: Axonemal dyneins are large AAA+ type motor proteins that exhibit unique motor properties during ciliary beating. This study established a mutation system for Tetrahymena outer arm dynein and characterized four nucleotide-binding loops (P-loops; P1-P4) in ...

    Abstract Axonemal dyneins are large AAA+ type motor proteins that exhibit unique motor properties during ciliary beating. This study established a mutation system for Tetrahymena outer arm dynein and characterized four nucleotide-binding loops (P-loops; P1-P4) in the alpha heavy chain (Dyh3p). Macronuclear transformation of the mutant DYH3 genes in DYH3-knockout (KO-DYH3) cells enabled P-loop mutations that abolish the ability of nucleotide binding to be stably maintained in the polyploid genome. This mutation system revealed that the P3 and P4 mutant dyneins rescued lethality in macronuclear KO-DYH3 cells and exhibited normal ciliary localization. Intriguingly, however, an in vitro motility assay showed that the P3 mutation abolished the motor activity of Dyh3p, whereas the P4 mutation did not affect the gliding velocity or gliding index of Dyh3p. In contrast, no P1 or P2 mutant cells were isolated from the KO-DYH3 cells, which suggests that nucleotide binding at the P1 and P2 sites is required for the intracellular function of Dyh3p. This mutation system will be useful for further molecular studies of diverse axonemal dyneins and ciliary motility.
    MeSH term(s) Amino Acid Sequence ; Animals ; Axonemal Dyneins/chemistry ; Axonemal Dyneins/genetics ; Axonemal Dyneins/metabolism ; Binding Sites ; Cilia/metabolism ; Gene Knockdown Techniques ; Genes, Protozoan ; Molecular Motor Proteins/chemistry ; Molecular Motor Proteins/genetics ; Molecular Motor Proteins/metabolism ; Mutation ; Protozoan Proteins/chemistry ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Sequence Homology, Amino Acid ; Tetrahymena thermophila/genetics ; Tetrahymena thermophila/metabolism
    Chemical Substances Molecular Motor Proteins ; Protozoan Proteins ; Axonemal Dyneins (EC 3.6.4.2)
    Language English
    Publishing date 2017-01-29
    Publishing country United States
    Document type Journal Article
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2017.01.020
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 116: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article ; Online: Identification of biotin carboxyl carrier protein in Tetrahymena and its application in in vitro motility systems of outer arm dynein.

    Edamatsu, Masaki

    Journal of microbiological methods

    2014  Volume 105, Page(s) 150–154

    Abstract: Axonemal dynein plays a central role in ciliary beating. Recently, a functional expression system of axonemal dynein was established in the ciliated protozoan Tetrahymena. This study identifies biotin carboxyl carrier protein (BCCP) in Tetrahymena and ... ...

    Abstract Axonemal dynein plays a central role in ciliary beating. Recently, a functional expression system of axonemal dynein was established in the ciliated protozoan Tetrahymena. This study identifies biotin carboxyl carrier protein (BCCP) in Tetrahymena and demonstrates its application in in vitro motility systems of outer arm dynein.
    MeSH term(s) Acetyl-CoA Carboxylase/analysis ; Acetyl-CoA Carboxylase/genetics ; Amino Acid Sequence ; Base Sequence ; Cluster Analysis ; Dyneins/metabolism ; Fatty Acid Synthase, Type II/analysis ; Fatty Acid Synthase, Type II/genetics ; Locomotion ; Models, Molecular ; Phylogeny ; Protein Conformation ; Sequence Homology, Amino Acid ; Tetrahymena/chemistry ; Tetrahymena/genetics ; Tetrahymena/physiology
    Chemical Substances Dyneins (EC 3.6.4.2) ; Fatty Acid Synthase, Type II (EC 6.-) ; Acetyl-CoA Carboxylase (EC 6.4.1.2) ; biotin carboxyl carrier protein (EC 6.4.1.2)
    Language English
    Publishing date 2014-10
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 604916-3
    ISSN 1872-8359 ; 0167-7012
    ISSN (online) 1872-8359
    ISSN 0167-7012
    DOI 10.1016/j.mimet.2014.07.036
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1849: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  6. Article ; Online: Motor domain-based motility system and motile properties of alpha heavy chain in Tetrahymena outer arm dynein.

    Edamatsu, Masaki

    Biochemical and biophysical research communications

    2014  Volume 453, Issue 3, Page(s) 595–599

    Abstract: Axonemal dynein plays an essential role in ciliary motility, and impaired ciliary motility causes human diseases such as primary ciliary dyskinesia (PCD). The motor domain of axonemal dynein powers ciliary motility and its function is regulated by ... ...

    Abstract Axonemal dynein plays an essential role in ciliary motility, and impaired ciliary motility causes human diseases such as primary ciliary dyskinesia (PCD). The motor domain of axonemal dynein powers ciliary motility and its function is regulated by several accessary proteins bound to the tail region. Therefore, to understand the essential properties of dynein motility, examining the motile properties of the motor domain without the tail is necessary. In this study, the functional motor domain of the alpha heavy chain in Tetrahymena outer arm dynein was purified, and its motile properties were examined using an in vitro motility system. The purified protein caused microtubules to glide at a velocity of 5.0μm/s with their minus-end trailing, and motility was inhibited in an ATP concentration-dependent manner, which is in contrast with kinesin1. This method could be applicable to other axonemal dyneins and will enable further molecular studies on diverse axonemal dyneins and ciliary motility.
    MeSH term(s) Dyneins/chemistry ; Dyneins/metabolism ; Microscopy, Fluorescence ; Polymerase Chain Reaction ; Tetrahymena/metabolism
    Chemical Substances Dyneins (EC 3.6.4.2)
    Language English
    Publishing date 2014-10-24
    Publishing country United States
    Document type Journal Article
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2014.09.127
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 116: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  7. Article ; Online: Bidirectional motility of the fission yeast kinesin-5, Cut7.

    Edamatsu, Masaki

    Biochemical and biophysical research communications

    2014  Volume 446, Issue 1, Page(s) 231–234

    Abstract: Kinesin-5 is a homotetrameric motor with its motor domain at the N-terminus. Kinesin-5 crosslinks microtubules and functions in separating spindle poles during mitosis. In this study, the motile properties of Cut7, fission yeast kinesin-5, were examined ... ...

    Abstract Kinesin-5 is a homotetrameric motor with its motor domain at the N-terminus. Kinesin-5 crosslinks microtubules and functions in separating spindle poles during mitosis. In this study, the motile properties of Cut7, fission yeast kinesin-5, were examined for the first time. In in vitro motility assays, full-length Cut7 moved toward minus-end of microtubules, but the N-terminal half of Cut7 moved toward the opposite direction. Furthermore, additional truncated constructs lacking the N-terminal or C-terminal regions, but still contained the motor domain, did not switch the motile direction. These indicated that Cut7 was a bidirectional motor, and microtubule binding regions at the N-terminus and C-terminus were not involved in its directionality.
    MeSH term(s) Binding Sites ; Cell Division ; Kinesin/chemistry ; Kinesin/genetics ; Kinesin/metabolism ; Microtubules/metabolism ; Movement ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Peptide Fragments/metabolism ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Schizosaccharomyces/cytology ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism
    Chemical Substances Cut7 protein, S pombe ; Peptide Fragments ; Recombinant Proteins ; Schizosaccharomyces pombe Proteins ; Kinesin (EC 3.6.4.4)
    Language English
    Publishing date 2014-03-28
    Publishing country United States
    Document type Journal Article
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2014.02.106
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 116: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  8. Article ; Online: The functional expression and motile properties of recombinant outer arm dynein from Tetrahymena.

    Edamatsu, Masaki

    Biochemical and biophysical research communications

    2014  Volume 447, Issue 4, Page(s) 596–601

    Abstract: Cilia and flagella are motile organelles that play various roles in eukaryotic cells. Ciliary movement is driven by axonemal dyneins (outer arm and inner arm dyneins) that bind to peripheral microtubule doublets. Elucidating the molecular mechanism of ... ...

    Abstract Cilia and flagella are motile organelles that play various roles in eukaryotic cells. Ciliary movement is driven by axonemal dyneins (outer arm and inner arm dyneins) that bind to peripheral microtubule doublets. Elucidating the molecular mechanism of ciliary movement requires the genetic engineering of axonemal dyneins; however, no expression system for axonemal dyneins has been previously established. This study is the first to purify recombinant axonemal dynein with motile activity. In the ciliated protozoan Tetrahymena, recombinant outer arm dynein purified from ciliary extract was able to slide microtubules in a gliding assay. Furthermore, the recombinant dynein moved processively along microtubules in a single-molecule motility assay. This expression system will be useful for investigating the unique properties of diverse axonemal dyneins and will enable future molecular studies on ciliary movement.
    MeSH term(s) Axonemal Dyneins/genetics ; Axonemal Dyneins/isolation & purification ; Axonemal Dyneins/physiology ; Cilia/physiology ; Flagella/physiology ; Genes, Protozoan ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/isolation & purification ; Green Fluorescent Proteins/metabolism ; Microtubules/physiology ; Movement/physiology ; Protozoan Proteins/genetics ; Protozoan Proteins/isolation & purification ; Protozoan Proteins/physiology ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/isolation & purification ; Recombinant Fusion Proteins/metabolism ; Tetrahymena/chemistry ; Tetrahymena/genetics ; Tetrahymena/physiology
    Chemical Substances Protozoan Proteins ; Recombinant Fusion Proteins ; Green Fluorescent Proteins (147336-22-9) ; Axonemal Dyneins (EC 3.6.4.2)
    Language English
    Publishing date 2014-05-16
    Publishing country United States
    Document type Journal Article
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2014.04.040
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 116: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  9. Article: Establishment of a mutation system in Tetrahymena outer arm dynein and P-loop functions of the alpha heavy chain (Dyh3p)

    Edamatsu, Masaki

    Biochemical and biophysical research communications. 2017 Jan. 29, v. 483

    2017  

    Abstract: Axonemal dyneins are large AAA+ type motor proteins that exhibit unique motor properties during ciliary beating. This study established a mutation system for Tetrahymena outer arm dynein and characterized four nucleotide-binding loops (P-loops; P1-P4) in ...

    Abstract Axonemal dyneins are large AAA+ type motor proteins that exhibit unique motor properties during ciliary beating. This study established a mutation system for Tetrahymena outer arm dynein and characterized four nucleotide-binding loops (P-loops; P1-P4) in the alpha heavy chain (Dyh3p). Macronuclear transformation of the mutant DYH3 genes in DYH3-knockout (KO-DYH3) cells enabled P-loop mutations that abolish the ability of nucleotide binding to be stably maintained in the polyploid genome. This mutation system revealed that the P3 and P4 mutant dyneins rescued lethality in macronuclear KO-DYH3 cells and exhibited normal ciliary localization. Intriguingly, however, an in vitro motility assay showed that the P3 mutation abolished the motor activity of Dyh3p, whereas the P4 mutation did not affect the gliding velocity or gliding index of Dyh3p. In contrast, no P1 or P2 mutant cells were isolated from the KO-DYH3 cells, which suggests that nucleotide binding at the P1 and P2 sites is required for the intracellular function of Dyh3p. This mutation system will be useful for further molecular studies of diverse axonemal dyneins and ciliary motility.
    Keywords Tetrahymena ; dynein ATPase ; genes ; molecular motor proteins ; mutants ; mutation ; polyploidy
    Language English
    Dates of publication 2017-0129
    Size p. 24-31.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2017.01.020
    Database NAL-Catalogue (AGRICOLA)

    More links

    Kategorien

    In stock of ZB MED Bonn / Germany

    Z 71/706: Show issues
    Z 3.8: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  10. Article: The M-Ras-RA-GEF-2-Rap1 pathway mediates tumor necrosis factor-alpha dependent regulation of integrin activation in splenocytes.

    Yoshikawa, Yoko / Satoh, Takaya / Tamura, Takashi / Wei, Ping / Bilasy, Shymaa E / Edamatsu, Hironori / Aiba, Atsu / Katagiri, Koko / Kinashi, Tatsuo / Nakao, Kazuki / Kataoka, Tohru

    Molecular biology of the cell

    2007  Volume 18, Issue 8, Page(s) 2949–2959

    Abstract: ... by the possession of a Ras/Rap1-associating domain, interacting with M-Ras-GTP as an effector, in addition ... hematopoietic cells, activated M-Ras potently induced lymphocyte function-associated antigen 1 (LFA-1)-mediated ... activated LFA-1 in a manner dependent on M-Ras, RA-GEF-2, and Rap1 and induced activation of M-Ras and Rap1 ...

    Abstract The Rap1 small GTPase has been implicated in regulation of integrin-mediated leukocyte adhesion downstream of various chemokines and cytokines in many aspects of inflammatory and immune responses. However, the mechanism for Rap1 regulation in the adhesion signaling remains unclear. RA-GEF-2 is a member of the multiple-member family of guanine nucleotide exchange factors (GEFs) for Rap1 and characterized by the possession of a Ras/Rap1-associating domain, interacting with M-Ras-GTP as an effector, in addition to the GEF catalytic domain. Here, we show that RA-GEF-2 is specifically responsible for the activation of Rap1 that mediates tumor necrosis factor-alpha (TNF-alpha)-triggered integrin activation. In BAF3 hematopoietic cells, activated M-Ras potently induced lymphocyte function-associated antigen 1 (LFA-1)-mediated cell aggregation. This activation was totally abrogated by knockdown of RA-GEF-2 or Rap1. TNF-alpha treatment activated LFA-1 in a manner dependent on M-Ras, RA-GEF-2, and Rap1 and induced activation of M-Ras and Rap1 in the plasma membrane, which was accompanied by recruitment of RA-GEF-2. Finally, we demonstrated that M-Ras and RA-GEF-2 were indeed involved in TNF-alpha-stimulated and Rap1-mediated LFA-1 activation in splenocytes by using mice deficient in RA-GEF-2. These findings proved a crucial role of the cross-talk between two Ras-family GTPases M-Ras and Rap1, mediated by RA-GEF-2, in adhesion signaling.
    MeSH term(s) Animals ; Cell Adhesion/drug effects ; Cell Aggregation/drug effects ; Enzyme Activation/drug effects ; Gene Targeting ; Guanine Nucleotide Exchange Factors/metabolism ; Humans ; Integrins/metabolism ; Intercellular Adhesion Molecule-1/metabolism ; Lymphocyte Function-Associated Antigen-1/metabolism ; Mice ; Models, Biological ; Monomeric GTP-Binding Proteins/metabolism ; Spleen/cytology ; Spleen/drug effects ; Tumor Necrosis Factor-alpha/pharmacology ; rap1 GTP-Binding Proteins/metabolism ; ras Proteins/metabolism
    Chemical Substances CNrasGEF protein, mouse ; Guanine Nucleotide Exchange Factors ; Integrins ; Lymphocyte Function-Associated Antigen-1 ; MRAS protein, human ; Tumor Necrosis Factor-alpha ; Intercellular Adhesion Molecule-1 (126547-89-5) ; Mras protein, mouse (EC 3.6.1.-) ; Monomeric GTP-Binding Proteins (EC 3.6.5.2) ; rap1 GTP-Binding Proteins (EC 3.6.5.2) ; ras Proteins (EC 3.6.5.2)
    Language English
    Publishing date 2007-08
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E07-03-0250
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 2853: 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.MO 410: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top