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  1. Article: Phosphorylation of annexin I by TRPM7 channel-kinase.

    Dorovkov, Maxim V / Ryazanov, Alexey G

    The Journal of biological chemistry

    2004  Volume 279, Issue 49, Page(s) 50643–50646

    Abstract: ... kinase. Phosphorylation of annexin 1 by TRPM7 kinase is stimulated by Ca2+ and is dramatically increased ... in extracts from cells overexpressing TRPM7. Phosphorylation of annexin 1 by TRPM7 kinase occurs at a conserved serine ... therefore, phosphorylation of annexin 1 at Ser5 by TRPM7 kinase may modulate function of annexin 1. ...

    Abstract TRPM7 is an unusual bifunctional molecule consisting of a TRP ion channel fused to a protein kinase domain. It has been shown that TRPM7 plays a key role in the regulation of intracellular magnesium homeostasis as well as in anoxic neuronal death. TRPM7 channel has been characterized using electrophysiological techniques; however, the function of the kinase domain is not known and endogenous substrates for the kinase have not been reported previously. Here we have identified annexin 1 as a substrate for TRPM7 kinase. Phosphorylation of annexin 1 by TRPM7 kinase is stimulated by Ca2+ and is dramatically increased in extracts from cells overexpressing TRPM7. Phosphorylation of annexin 1 by TRPM7 kinase occurs at a conserved serine residue (Ser5) located within the N-terminal amphipathic alpha-helix of annexin 1. The N-terminal region plays a crucial role in interaction of annexin 1 with other proteins and membranes, and therefore, phosphorylation of annexin 1 at Ser5 by TRPM7 kinase may modulate function of annexin 1.
    MeSH term(s) Amino Acid Sequence ; Animals ; Annexin A1/chemistry ; Binding Sites ; Calcium/chemistry ; Cathepsin D/pharmacology ; Cell Line ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; Humans ; Ion Channels/metabolism ; Ion Channels/physiology ; Ions ; Magnesium/chemistry ; Membrane Proteins/metabolism ; Membrane Proteins/physiology ; Mice ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Peptides/chemistry ; Phosphorylation ; Polymerase Chain Reaction ; Protein Binding ; Protein Kinases/metabolism ; Protein Kinases/physiology ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry ; Sequence Homology, Amino Acid ; Serine/chemistry ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; TRPM Cation Channels ; Trypsin/pharmacology
    Chemical Substances Annexin A1 ; Ion Channels ; Ions ; Membrane Proteins ; Peptides ; Recombinant Proteins ; TRPM Cation Channels ; Serine (452VLY9402) ; Protein Kinases (EC 2.7.-) ; Trpm7 protein, mouse (EC 2.7.1.-) ; Trypsin (EC 3.4.21.4) ; Cathepsin D (EC 3.4.23.5) ; Magnesium (I38ZP9992A) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2004-10-12
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.C400441200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  2. Article ; Online: Phosphorylation of annexin A1 by TRPM7 kinase: a switch regulating the induction of an α-helix.

    Dorovkov, Maxim V / Kostyukova, Alla S / Ryazanov, Alexey G

    Biochemistry

    2011  Volume 50, Issue 12, Page(s) 2187–2193

    Abstract: ... ion channel. Previously, we have identified annexin A1 as a substrate for TRPM7 kinase and found that TRPM7 ... TRPM7 is an unusual bifunctional protein consisting of an α-kinase domain fused to a TRP ... phosphorylates annexin A1 at Ser5 within the N-terminal α-helix. Annexin A1 is a Ca(2+)-dependent membrane ...

    Abstract TRPM7 is an unusual bifunctional protein consisting of an α-kinase domain fused to a TRP ion channel. Previously, we have identified annexin A1 as a substrate for TRPM7 kinase and found that TRPM7 phosphorylates annexin A1 at Ser5 within the N-terminal α-helix. Annexin A1 is a Ca(2+)-dependent membrane binding protein, which has been implicated in membrane trafficking and reorganization. The N-terminal tail of annexin A1 can interact with either membranes or S100A11 protein, and it adopts the conformation of an amphipathic α-helix upon these interactions. Moreover, the existing evidence indicates that the formation of an α-helix is essential for these interactions. Here we show that phosphorylation at Ser5 prevents the N-terminal peptide of annexin A1 from adopting an α-helical conformation in the presence of membrane-mimetic micelles as well as phospholipid vesicles. We also show that phosphorylation at Ser5 dramatically weakens the binding of the peptide to S100A11. Our data suggest that phosphorylation at Ser5 regulates the interaction of annexin A1 with membranes as well as S100A11 protein.
    MeSH term(s) Amino Acid Sequence ; Animals ; Annexin A1/chemistry ; Annexin A1/metabolism ; Cell Membrane/metabolism ; Molecular Sequence Data ; Peptide Fragments/chemistry ; Peptide Fragments/metabolism ; Phosphorylation ; Protein Structure, Secondary ; S100 Proteins/metabolism ; Serine ; TRPM Cation Channels/metabolism
    Chemical Substances Annexin A1 ; Peptide Fragments ; S100 Proteins ; TRPM Cation Channels ; Serine (452VLY9402)
    Language English
    Publishing date 2011-02-18
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/bi101963h
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 217: 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)

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