A scanning peptide array approach uncovers association sites within the JNK/βarrestin signalling complex

βarrestins are molecular scaffolds that can bring together three-component mitogen-activated protein kinase signalling modules to promote signal compartmentalisation. We use peptide array technology to define novel interfaces between components within the c-Jun N-terminal kinase (JNK)/βarrestin sign...

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Veröffentlicht in:	FEBS letters 2009-10, Vol.583 (20), p.3310-3316
Hauptverfasser:	Li, Xiang, MacLeod, Ruth, Dunlop, Allan J., Edwards, Helen V., Advant, Noopur, Gibson, Lucien C.D., Devine, Nicola M., Brown, Kim M., Adams, David R., Houslay, Miles D., Baillie, George S.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals apoptosis signal-regulating kinase 1 Arrestin Arrestins - chemistry Arrestins - genetics Arrestins - metabolism ASK1 beta-Arrestins c-Jun N-terminal kinase CD site common docking site JNK Map kinase MAP Kinase Kinase 4 - chemistry MAP Kinase Kinase 4 - genetics MAP Kinase Kinase 4 - metabolism MAP Kinase Signaling System - physiology MAPK MAPK kinase 4 Mitogen-Activated Protein Kinase 10 - chemistry Mitogen-Activated Protein Kinase 10 - genetics Mitogen-Activated Protein Kinase 10 - metabolism MKK4 Models, Molecular Molecular Sequence Data Peptide array Peptide Library Peptides - genetics Peptides - metabolism Protein Array Analysis - methods Protein Binding Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Scaffold
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Zusammenfassung:	βarrestins are molecular scaffolds that can bring together three-component mitogen-activated protein kinase signalling modules to promote signal compartmentalisation. We use peptide array technology to define novel interfaces between components within the c-Jun N-terminal kinase (JNK)/βarrestin signalling complex. We show that βarrestin 1 and βarrestin 2 associate with JNK3 via the kinase N-terminal domain in a region that, surprisingly, does not harbour a known ‘common docking’ motif. In the N-domain and C-terminus of βarrestin 1 and βarrestin 2 we identify two novel apoptosis signal-regulating kinase 1 binding sites and in the N-domain of the βarrestin 1 and βarrestin 2 we identify a novel MKK4 docking site. MINT-7263196, MINT-7263175: Arrestin beta-2 (uniprotkb:P32121) binds (MI:0407) to ASK1 (uniprotkb:Q99683) by peptide array (MI:0081) MINT-7263136: JNK3 (uniprotkb:P53779) binds (MI:0407) to Arrestin beta-1 (uniprotkb:P49407) by peptide array (MI:0081) MINT-7263161: JNK3 (uniprotkb:P53779) binds (MI:0407) to Arrestin beta-2 (uniprotkb:P32121) by peptide array (MI:0081) MINT-7263304: Arrestin beta-1 (uniprotkb:P49407) physically interacts (MI:0915) with ASK1 (uniprotkb:Q99683) by anti tag coimmunoprecipitation (MI:0007) MINT-7263286: Arrestin beta-2 (uniprotkb:P32121) binds (MI:0407) to MKK4 (uniprotkb:P45985) by peptide array (MI:0081) MINT-7263231, MINT-7263254: Arrestin beta-1 (uniprotkb:P49407) binds (MI:0407) to ASK1 (uniprotkb:Q99683) by peptide array (MI:0081) MINT-7263269: Arrestin beta-1 (uniprotkb:P49407) binds (MI:0407) to MKK4 (uniprotkb:P45985) by peptide array (MI:0081)
ISSN:	0014-5793 1873-3468
DOI:	10.1016/j.febslet.2009.09.035