Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding

被引：0
|
作者：
Irene Díaz-Moreno
David Hollingworth
Thomas A Frenkiel
Geoff Kelly
Stephen Martin
Steven Howell
MaríaFlor García-Mayoral
Roberto Gherzi
Paola Briata
Andres Ramos
机构：
[1] MRC National Institute for Medical Research,Molecular Structure Division
[2] The Ridgeway,Physical Biochemistry Division
[3] Mill Hill,undefined
[4] MRC Biomedical NMR Centre,undefined
[5] The Ridgeway,undefined
[6] Mill Hill,undefined
[7] MRC National Institute for Medical Research,undefined
[8] The Ridgeway,undefined
[9] Mill Hill,undefined
[10] Istituto Nazionale per la Ricerca sul Cancro,undefined
[11] Largo Benzi Rosanna,undefined
[12] 10,undefined
[13] Instituto de Bioquímica Vegetal y Fotosíntesis,undefined
[14] US-CSIC,undefined
[15] Avda. Americo Vespucio 49,undefined
来源：
Nature Structural & Molecular Biology | 2009年 / 16卷
关键词：
D O I：
暂无
中图分类号：
学科分类号：
摘要：
KSRP is involved in mRNA instability, a role that is repressed upon AKT kinase–mediated phosphorylation, which promotes 14-3-3 interaction. This modification site is now shown to be exposed upon AKT phosphorylation through unfolding of the KH1 domain of KSRP, an event that allows 14-3-3 interaction, which in turn affects nuclear cytoplasmic partitioning.
引用
收藏
页码：238 / 246
页数：8
相关论文
共 50 条
  • [11] Primate-specific isoform of Nedd4-1 regulates substrate binding via Ser/Thr phosphorylation and 14-3-3 binding
    George Kefalas
    Daniela Rotin
    Scientific Reports, 13
  • [12] The Serine/Threonine kinase Par1b regulates ORP3 localization via 14-3-3 binding.
    Fernandez, D. M.
    Lazaro-Dieguez, F.
    Muesch, A.
    MOLECULAR BIOLOGY OF THE CELL, 2014, 25
  • [13] Binding of 14-3-3β but not 14-3-3σ controls the cytoplasmic localization of CDC25B:: binding site preferences of 14-3-3 subtypes and the subcellular localization of CDC25B
    Uchida, S
    Kuma, A
    Ohtsubo, M
    Shimura, M
    Hirata, M
    Nakagama, H
    Matsunaga, T
    Ishizaka, Y
    Yamashita, K
    JOURNAL OF CELL SCIENCE, 2004, 117 (14) : 3011 - 3020
  • [14] Binding of 14-3-3β regulates the kinase activity and subcellular localization of testicular protein kinase 1
    Toshima, JY
    Toshima, J
    Mizuno, K
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (46) : 43471 - 43481
  • [15] Structural Modulation of Phosducin by Phosphorylation and 14-3-3 Protein Binding
    Rezabkova, Lenka
    Kacirova, Miroslava
    Sulc, Miroslav
    Herman, Petr
    Vecer, Jaroslav
    Stepanek, Miroslav
    Obsilova, Veronika
    Obsil, Tomas
    BIOPHYSICAL JOURNAL, 2012, 103 (09) : 1960 - 1969
  • [16] Phosphorylation of Grb10 regulates its interaction with 14-3-3
    Urschel, S
    Bassermann, F
    Bai, RY
    Münch, S
    Peschel, C
    Duyster, J
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (17) : 16987 - 16993
  • [17] 14-3-3 is phosphorylated by casein kinase I on residue 233 - Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction
    Dubois, T
    Rommel, C
    Howell, S
    Steinhussen, U
    Soneji, Y
    Morrice, N
    Moelling, R
    Aitken, A
    JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (46) : 28882 - 28888
  • [18] Promotion of importin α-mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3
    Faul, C
    Hüttelmaier, S
    Oh, J
    Hachet, V
    Singer, RH
    Mundel, P
    JOURNAL OF CELL BIOLOGY, 2005, 169 (03): : 415 - 424
  • [19] Mutation of the keratin phosphorylation site that regulates 14-3-3 binding reorganizes keratin filaments in transgenic mice.
    Ku, NO
    Omary, MB
    MOLECULAR BIOLOGY OF THE CELL, 1999, 10 : 135A - 135A
  • [20] Regulation of Nox1 activity via protein kinase A-mediated phosphorylation of NoxA1 and 14-3-3 binding
    Kim, Jun-Sub
    Diebold, Becky A.
    Babior, Bernard M.
    Knaus, Ulla G.
    Bokoch, Gary M.
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (48) : 34787 - 34800
12345