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  1. Article: TRPM7, a novel regulator of actomyosin contractility and cell adhesion.

    Clark, Kristopher / Langeslag, Michiel / van Leeuwen, Bart / Ran, Leonie / Ryazanov, Alexey G / Figdor, Carl G / Moolenaar, Wouter H / Jalink, Kees / van Leeuwen, Frank N

    The EMBO journal

    2006  Volume 25, Issue 2, Page(s) 290–301

    Abstract: ... adhesion and migration. While in lower eukaryotes, alpha-kinases control actomyosin relaxation, a similar ... and -independent pathways on actomyosin contractility. ... Actomyosin contractility regulates various cell biological processes including cytokinesis ...

    Abstract Actomyosin contractility regulates various cell biological processes including cytokinesis, adhesion and migration. While in lower eukaryotes, alpha-kinases control actomyosin relaxation, a similar role for mammalian alpha-kinases has yet to be established. Here, we examined whether TRPM7, a cation channel fused to an alpha-kinase, can affect actomyosin function. We demonstrate that activation of TRPM7 by bradykinin leads to a Ca(2+)- and kinase-dependent interaction with the actomyosin cytoskeleton. Moreover, TRPM7 phosphorylates the myosin IIA heavy chain. Accordingly, low overexpression of TRPM7 increases intracellular Ca2+ levels accompanied by cell spreading, adhesion and the formation of focal adhesions. Activation of TRPM7 induces the transformation of these focal adhesions into podosomes by a kinase-dependent mechanism, an effect that can be mimicked by pharmacological inhibition of myosin II. Collectively, our results demonstrate that regulation of cell adhesion by TRPM7 is the combined effect of kinase-dependent and -independent pathways on actomyosin contractility.
    MeSH term(s) Actomyosin/metabolism ; Actomyosin/physiology ; Animals ; Calcium/metabolism ; Cell Adhesion/physiology ; Cell Line ; Cytoskeleton/metabolism ; Humans ; Immunoprecipitation ; Mice ; Microscopy, Fluorescence ; Nonmuscle Myosin Type IIA/metabolism ; Phosphorylation ; Phosphotransferases/metabolism ; Protein-Serine-Threonine Kinases ; TRPM Cation Channels/metabolism
    Chemical Substances TRPM Cation Channels ; Actomyosin (9013-26-7) ; Phosphotransferases (EC 2.7.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; TRPM7 protein, human (EC 2.7.11.1) ; Nonmuscle Myosin Type IIA (EC 3.6.1.-) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2006-01-25
    Publishing country England
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.1038/sj.emboj.7600931
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1808: Show issues Location:
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    Zs.MG 100: Show issues

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  2. Article ; Online: TRPM7 triggers Ca2+ sparks and invadosome formation in neuroblastoma cells.

    Visser, Daan / Langeslag, Michiel / Kedziora, Katarzyna M / Klarenbeek, Jeffrey / Kamermans, Alwin / Horgen, F David / Fleig, Andrea / van Leeuwen, Frank N / Jalink, Kees

    Cell calcium

    2013  Volume 54, Issue 6, Page(s) 404–415

    Abstract: ... affects actomyosin contractility and the formation of cell adhesions such as invadosomes and ... controlled by actomyosin contractility and local Ca2+ signals. The divalent cation channel TRPM7 (Transient ... from TRPM7-mediated Ca2+ sparks. Rather, our data indicate that TRPM7 affects actomyosin contractility and ...

    Abstract Cell migration depends on the dynamic formation and turnover of cell adhesions and is tightly controlled by actomyosin contractility and local Ca2+ signals. The divalent cation channel TRPM7 (Transient Receptor Potential cation channel, subfamily Melastatin, member 7) has recently received much attention as a regulator of cell adhesion, migration and (localized) Ca2+ signaling. Overexpression and knockdown of TRPM7 affects actomyosin contractility and the formation of cell adhesions such as invadosomes and focal adhesions, but the role of TRPM7-mediated Ca2+ signals herein is currently not understood. Using Total Internal Reflection Fluorescence (TIRF) Ca2+ fluorometry and a novel automated analysis routine we have addressed the role of Ca2+ in the control of invadosome dynamics in N1E-115 mouse neuroblastoma cells. We find that TRPM7 promotes the formation of highly repetitive and localized Ca2+ microdomains or "Ca2+ sparking hotspots" at the ventral plasma membrane. Ca2+ sparking appears strictly dependent on extracellular Ca2+ and is abolished by TRPM7 channel inhibitors such as waixenicin-A. TRPM7 inhibition also induces invadosome dissolution. However, invadosome formation is (functionally and spatially) dissociated from TRPM7-mediated Ca2+ sparks. Rather, our data indicate that TRPM7 affects actomyosin contractility and invadosome formation independent of Ca2+ influx.
    MeSH term(s) Acetates/pharmacology ; Actomyosin/metabolism ; Animals ; Calcium/metabolism ; Calcium Signaling ; Cell Adhesion/drug effects ; Cell Line, Tumor ; Cell Membrane/metabolism ; Cell Movement/drug effects ; Diterpenes/pharmacology ; Mice ; Neuroblastoma/metabolism ; Neuroblastoma/pathology ; RNA Interference ; RNA, Small Interfering/metabolism ; TRPM Cation Channels/antagonists & inhibitors ; TRPM Cation Channels/genetics ; TRPM Cation Channels/metabolism
    Chemical Substances Acetates ; Diterpenes ; RNA, Small Interfering ; TRPM Cation Channels ; waixenicin A ; Actomyosin (9013-26-7) ; Trpm7 protein, mouse (EC 2.7.1.-) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2013-10-16
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 757687-0
    ISSN 1532-1991 ; 0143-4160
    ISSN (online) 1532-1991
    ISSN 0143-4160
    DOI 10.1016/j.ceca.2013.09.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1596: 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: TRPM7 triggers Ca2+ sparks and invadosome formation in neuroblastoma cells

    Visser, Daan / Langeslag, Michiel / Kedziora, Katarzyna M / Klarenbeek, Jeffrey / Kamermans, Alwin / Horgen, F. David / Fleig, Andrea / van Leeuwen, Frank N / Jalink, Kees

    Cell calcium. 2013 Dec., v. 54, no. 6

    2013  

    Abstract: ... affects actomyosin contractility and the formation of cell adhesions such as invadosomes and ... controlled by actomyosin contractility and local Ca2+ signals. The divalent cation channel TRPM7 (Transient ... from TRPM7-mediated Ca2+ sparks. Rather, our data indicate that TRPM7 affects actomyosin contractility and ...

    Abstract Cell migration depends on the dynamic formation and turnover of cell adhesions and is tightly controlled by actomyosin contractility and local Ca2+ signals. The divalent cation channel TRPM7 (Transient Receptor Potential cation channel, subfamily Melastatin, member 7) has recently received much attention as a regulator of cell adhesion, migration and (localized) Ca2+ signaling. Overexpression and knockdown of TRPM7 affects actomyosin contractility and the formation of cell adhesions such as invadosomes and focal adhesions, but the role of TRPM7-mediated Ca2+ signals herein is currently not understood. Using Total Internal Reflection Fluorescence (TIRF) Ca2+ fluorometry and a novel automated analysis routine we have addressed the role of Ca2+ in the control of invadosome dynamics in N1E-115 mouse neuroblastoma cells. We find that TRPM7 promotes the formation of highly repetitive and localized Ca2+ microdomains or “Ca2+ sparking hotspots” at the ventral plasma membrane. Ca2+ sparking appears strictly dependent on extracellular Ca2+ and is abolished by TRPM7 channel inhibitors such as waixenicin-A. TRPM7 inhibition also induces invadosome dissolution. However, invadosome formation is (functionally and spatially) dissociated from TRPM7-mediated Ca2+ sparks. Rather, our data indicate that TRPM7 affects actomyosin contractility and invadosome formation independent of Ca2+ influx.
    Keywords calcium ; calcium signaling ; cell adhesion ; cell movement ; fluorescence ; fluorometry ; mice ; plasma membrane
    Language English
    Dates of publication 2013-12
    Size p. 404-415.
    Publishing place Elsevier India Pvt Ltd.
    Document type Article
    ZDB-ID 757687-0
    ISSN 1532-1991 ; 0143-4160
    ISSN (online) 1532-1991
    ISSN 0143-4160
    DOI 10.1016/j.ceca.2013.09.003
    Database NAL-Catalogue (AGRICOLA)

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1596: 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.

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