Switches.ELM

Switch #:

SWTI000684

Switch type:
Binary

Switch subtype:
Physicochemical compatibility

Description:
Phosphorylation of Y170 in the WW-binding motif of Transcription factor AP-1 (Jun) by Tyrosine-protein kinase ABL1 (Abl1) blocks binding to the E3 ubiquitin-protein ligase Itchy (Itch). As a result, Transcription factor AP-1 (Jun) is not ubiquitylated by E3 ubiquitin-protein ligase Itchy (Itch), and thus not targeted for proteasomal degradation. Regulation of transcriptional activity of Transcription factor AP-1 (Jun) by Tyrosine-protein kinase ABL1 (Abl1) required translocation of the kinase to the nucleus, which was triggered by T cell activation.

Participants:
(1) Transcription factor AP-1 (Jun)
(2) E3 ubiquitin-protein ligase Itchy (Itch)

Interactions

Interaction #1 Jun - Itch

Interfaces
(1) LIG_WW_1 motif (₁₆₇PPVY₁₇₀) in Transcription factor AP-1 (Jun)
(2) WW domain_(289-318) and _(321-350) and _(401-430) and _(441-470) in E3 ubiquitin-protein ligase Itchy (Itch)

Interaction Regulation
PTM-dependent Abrogation (Phosphorylation of Y₁₇₀ on Transcription factor AP-1 (Jun)) of the Transcription factor AP-1 (Jun) LIG_WW_1 motif - E3 ubiquitin-protein ligase Itchy (Itch) WW domain interaction

Regulatory Enzymes for switch
Modifying enzymes for residue: Y₁₇₀: Tyrosine-protein kinase ABL1 (Abl1)

Context

References

(1) The tyrosine kinase c-Abl protects c-Jun from ubiquitination-mediated degradation in T cells.
Gao et al. J. Biol. Chem. (2006)