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Review article

Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes

Carol MACKINTOSH
Biochemical Journal Jul 06, 2004, 381 (2) 329-342; DOI: 10.1042/BJ20031332
Carol MACKINTOSH
MRC Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, U.K.
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Abstract

14-3-3 proteins exert an extraordinarily widespread influence on cellular processes in all eukaryotes. They operate by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. In these ways, 14-3-3s ‘finish the job’ when phosphorylation alone lacks the power to drive changes in the activities of intracellular proteins. By interacting dynamically with phosphorylated proteins, 14-3-3s often trigger events that promote cell survival – in situations from preventing metabolic imbalances caused by sudden darkness in leaves to mammalian cell-survival responses to growth factors. Recent work linking specific 14-3-3 isoforms to genetic disorders and cancers, and the cellular effects of 14-3-3 agonists and antagonists, indicate that the cellular complement of 14-3-3 proteins may integrate the specificity and strength of signalling through to different cellular responses.

  • 14-3-3 protein
  • cancer
  • cell signalling
  • neurodegenerative disorder
  • plant
  • protein kinase B (PKB)

Abbreviations: AANAT, arylalkamine/serotonin N-acetyltransferase; BAD, Bcl-2/Bcl-XL-antagonist, causing cell death; BSE, bovine spongiform encephalopathy; Cdc, cell-division cycle; CDK, cyclin-dependent kinase; chk, checkpoint kinase; CJD, Creutzfeldt–Jakob disease; COPI, coatamer I; CSF, cerebrospinal fluid; ER, endoplasmic reticulum; ERK, extracellular-signal-regulated kinase; FKHR, Forkhead in rhabdomyosarcoma; FOXO, Forkhead box, class O; HCV, hepatitis C virus; IRS-1, insulin receptor substrate-1; LR, axis, left–right axis; MAPK, mitogen-activated protein kinase; MDS, Miller–Dieker syndrome; NLS, nuclear localization signal; NR, nitrate reductase; PDE3B, phosphodiesterase 3B; PI3K, phosphoinositide 3-kinase; PKA, protein kinase A; PKB, protein kinase B; PKC, protein kinase C; SCA, spinocerebellar ataxia; SH2, Src homology 2; SnRK, SNF1-related kinase; TSE, transmissible spongiform encephalopathy; WPK4, wheat protein kinase 4

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July 2004

Volume: 381 Issue: 2

Biochemical Journal: 381 (2)
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Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
Carol MACKINTOSH
Biochemical Journal Jul 2004, 381 (2) 329-342; DOI: 10.1042/BJ20031332
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Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
Carol MACKINTOSH
Biochemical Journal Jul 2004, 381 (2) 329-342; DOI: 10.1042/BJ20031332

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  • Article
    • Abstract
    • INTRODUCTION
    • 14-3-3s ARE DIMERS, SO ARE THEY SIMPLE ADAPTERS?
    • 14-3-3s AS MULTIPURPOSE ‘CONFORMATION CLAMPS’
    • 14-3-3s COMPETE WITH OTHER BINDING PROTEINS TO CONTROL LOCATION AND ACTIVITY OF TARGETS
    • DEFINING THE 14-3-3-INTERACTING PHOSPHOPROTEOME – CLUSTERS AND THEMES
    • COMMON SIGNALS REGULATE SUBSETS OF 14-3-3-INTERACTING PROTEINS
    • 14-3-3s OPERATE TO COUNTERACT THE DANGERS OF SUDDEN DARKNESS IN LEAVES
    • A BREAKTHROUGH IN IDENTIFYING PKB (PROTEIN KINASE B) SUBSTRATES IN MAMMALIAN CELLS?
    • 14-3-3s IN CARCINOGENESIS AND CANCER THERAPY
    • 14-3-3s ACTIVATE p53 AND 14-3-3σ IS A p53 TARGET GENE
    • THE 14-3-3σ PARADOX OPENS A CHINK IN THE ARMOUR OF CANCERS
    • EXPERIMENTAL 14-3-3 ANTAGONISTS
    • 14-3-3s AS TARGETS OF PATHOGENIC PROTEINS AND TOXINS
    • 14-3-3s IN BRAIN DEVELOPMENT AND NEURODEGENERATIVE DISEASES
    • REDUNDANCY, SPECIFICITY AND REGULATION OF 14-3-3 ISOFORMS
    • Acknowledgments
    • References
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Keywords

14-3-3 protein
cancer
cell signalling
neurodegenerative disorder
plant
protein kinase B (PKB)

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