Pellino Proteins Contain a Cryptic FHA Domain that Mediates Interaction with Phosphorylated IRAK1 (Q27653149)

2

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Karl R Schmitz

3

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Liselotte E Jensen

4

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Kathryn M Ferguson

Diphosphothreonine-specific interaction between an SQ/TQ cluster and an FHA domain in the Rad53-Dun1 kinase cascade

5

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publication date

10 December 2008

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published in

Structure

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volume

16

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issue

12

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page(s)

1806-16

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cites work

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Pellino 3b negatively regulates interleukin-1-induced TAK1-dependent NF kappaB activation

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Interleukin-1 (IL-1) induces the Lys63-linked polyubiquitination of IL-1 receptor-associated kinase 1 to facilitate NEMO binding and the activation of IkappaBalpha kinase

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Characterization of Pellino2, a substrate of IRAK1 and IRAK4

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Pellino2 activates the mitogen activated protein kinase pathway

20 March 2017

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Pellino 1 is required for interleukin-1 (IL-1)-mediated signaling through its interaction with the IL-1 receptor-associated kinase 4 (IRAK4)-IRAK-tumor necrosis factor receptor-associated factor 6 (TRAF6) complex

20 March 2017

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20 March 2017

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Solution structure of the yeast Rad53 FHA2 complexed with a phosphothreonine peptide pTXXL: comparison with the structures of FHA2-pYXL and FHA1-pTXXD complexes

20 March 2017

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Solution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53

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BCL10 mediates lipopolysaccharide/toll-like receptor-4 signaling through interaction with Pellino2

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The IRAK-catalysed activation of the E3 ligase function of Pellino isoforms induces the Lys63-linked polyubiquitination of IRAK1.

29 September 2017

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29 September 2017

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29 September 2017

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