Switch #:
SWTI000660
Switch type:
Specificity
Switch subtype:
Competition

Description:
The WW-binding motif for Dystrophin (DMD) and the SH3-binding motif for Growth factor receptor-bound protein 2 (GRB2) on Dystroglycan (DAG1) overlap, making their interactions mutually exclusive and competitive.

Participants:
(1) Dystroglycan (DAG1)
(2) Dystrophin (DMD)
(3) Growth factor receptor-bound protein 2 (GRB2)

Interactions
Interaction #1 DAG1 - DMD

Is mutually exclusive with

Interfaces
(1) LIG_WW_1 motif (889PPPY892) in Dystroglycan (DAG1)
(2) WW domain (3057-3086) in Dystrophin (DMD)

Interaction Regulation
Effector binding Inhibition (Growth factor receptor-bound protein 2 (GRB2)) of the Dystroglycan (DAG1) LIG_WW_1 motif - Dystrophin (DMD) WW domain interaction

Additional Information
Structural information: 1EG4
Switch_Notes: Already in as SWTI000341
Interaction #2 DAG1 - GRB2

Is mutually exclusive with

Interfaces
(3) LIG_SH3_3 motif (888SPPPYVP894) in Dystroglycan (DAG1)
(4) SH3 domain (162-207) in Growth factor receptor-bound protein 2 (GRB2)

Interaction Regulation
Effector binding Inhibition (Dystrophin (DMD)) of the Dystroglycan (DAG1) LIG_SH3_3 motif - Growth factor receptor-bound protein 2 (GRB2) SH3 domain interaction

Additional Information
Switch_Notes: Already in as SWTI000341
Context
Switch localisation
ELM curated: cytosol, integral membrane protein, integral plasma membrane protein, focal adhesion, plasma membrane
Inferred: cytoskeleton, sarcolemma, cytosol, dystrophin-associated glycoprotein complex, costamere
References

(1) Characterization of the beta-dystroglycan-growth factor receptor 2 (Grb2) interaction.
Russo et al. Biochem. Biophys. Res. Commun. (2000)

(2) Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan.
Huang et al. Nat. Struct. Biol. (2000)

(3) Dystroglycan versatility in cell adhesion: a tale of multiple motifs.
Moore et al. Cell Commun. Signal (2010)




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