FEBS Letters
Volume 583, Issue 13 , Pages 2187-2193, 7 July 2009

Interaction specificity of Arabidopsis 14-3-3 proteins with phototropin receptor kinases

Edited by Miguel De la Rosa

  • Stuart Sullivan
    • ,
  • Catriona E. Thomson

      Affiliations

    • Present address: BioOutsource Ltd., Technology Terrace, West of Scotland Science Park, Glasgow G20 0XA, UK.
    • ,
  • Eirini Kaiserli

      Affiliations

    • Present address: The Salk Institute for Biological Studies, 10010 N. Torrey Pines Road, La Jolla, CA 92037, USA.
    • ,
  • John M. Christie

      Affiliations

    • Corresponding Author InformationCorresponding author.

Plant Science Group, Division of Molecular and Cellular Biology, Faculty of Biomedical and Life Sciences, University of Glasgow, University Avenue, Glasgow G12 8QQ, UK

Received 30 April 2009; received in revised form 2 June 2009; accepted 6 June 2009. published online 12 June 2009.

Abstract 

Phototropin receptor kinases play an important role in optimising plant growth in response to blue light. Much is known regarding their photochemical reactivity, yet little progress has been made to identify downstream signalling components. Here, we isolated several interacting proteins for Arabidopsis phototropin 1 (phot1) by yeast two-hybrid screening. These include members of the NPH3/RPT2 (NRL) protein family, proteins associated with vesicle trafficking, and the 14-3-3 lambda (λ) isoform from Arabidopsis. 14-3-3λ and phot1 were found to colocalise and interact in vivo. Moreover, 14-3-3 binding to phot1 was limited to non-epsilon 14-3-3 isoforms and was dependent on key sites of receptor autophosphorylation. No 14-3-3 binding was detected for Arabidopsis phot2, suggesting that 14-3-3 proteins are specific to phot1 signalling.

Structured summary

MINT-7146953: PHOT1 (uniprotkb:O48963) physically interacts (MI:0915) with ARF7 (uniprotkb:Q9LFJ7) by two hybrid (MI:0018)

MINT-7147335: PHOT1 (uniprotkb:O48963) physically interacts (MI:0914) with 14-3-3 phi (uniprotkb:P46077) by far Western blotting (MI:0047)

MINT-7146854: PHOT1 (uniprotkb:O48963) physically interacts (MI:0915) with RPT2 (uniprotkb:Q682S0) by two hybrid (MI:0018)

MINT-7147215: PHOT1 (uniprotkb:O48963) physically interacts (MI:0914) with 14-3-3 lambda (uniprotkb:P48349) by anti tag coimmunoprecipitation (MI:0007)

MINT-7147044, MINT-7147185, MINT-7147200, MINT-7147413: PHOT1 (uniprotkb:O48963) physically interacts (MI:0914) with 14-3-3 lambda (uniprotkb:P48349) by far Western blotting (MI:0047)

MINT-7146983: PHOT1 (uniprotkb:O48963) physically interacts (MI:0915) with 14-3-3 lambda (uniprotkb:P48349) by two hybrid (MI:0018)

MINT-7146871: PHOT1 (uniprotkb:O48963) physically interacts (MI:0915) with NPH3-like (uniprotkb:Q9S9Q9) by two hybrid (MI:0018)

MINT-7146905: PHOT1 (uniprotkb:O48963) physically interacts (MI:0915) with ARF2 (uniprotkb:Q9M1P5) by two hybrid (MI:0018)

MINT-7147364: PHOT1 (uniprotkb:O48963) physically interacts (MI:0914) with 14-3-3 upsilon (uniprotkb:P42645) by far Western blotting (MI:0047)

MINT-7147234: PHOT1 (uniprotkb:O48963) physically interacts (MI:0914) with 14-3-3 kappa (uniprotkb:P48348) by far Western blotting (MI:0047)

Keywords: 14-3-3 Protein, Signalling, Protein phosphorylation, Photoreceptor, Kinase activity, Protein–protein interaction, Arabidopsis thaliana

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PII: S0014-5793(09)00453-0

doi:10.1016/j.febslet.2009.06.011

FEBS Letters
Volume 583, Issue 13 , Pages 2187-2193, 7 July 2009

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