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Altered binding specificity

Adhesion-dependent phosphorylation of Y892 in Dystroglycan (DAG1) by Src kinase (Proto-oncogene tyrosine-protein kinase Src (SRC)) switches the specificity of DAG1 from the WW domain containing cytoskeletal linker Dystrophin (DMD) to the SH2 domain containing Tyrosine-protein kinase Fyn (FYN).

(1) Dystroglycan (DAG1)
(2) Dystrophin (DMD)
(3) Tyrosine-protein kinase Fyn (FYN)

Interaction #1 DAG1 - DMD

Is mutually exclusive with Interaction #2 DAG1 - FYN

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

Interaction Regulation
PTM-dependent Abrogation (Phosphorylation of Y892 on Dystroglycan (DAG1)) of the Dystroglycan (DAG1) LIG_WW_1 motif - Dystrophin (DMD) WW domain interaction

Additional Information
Structural information: 1EG4
Interaction #2 DAG1 - FYN

Is mutually exclusive with Interaction #1 DAG1 - DMD

(3) LIG_SH2_SRC motif (892YVPP895) in Dystroglycan (DAG1)
(4) SH2 domain (149-231) in Tyrosine-protein kinase Fyn (FYN)

Interaction Regulation
PTM-dependent Induction (Phosphorylation of Y892 on Dystroglycan (DAG1)) of the Dystroglycan (DAG1) LIG_SH2_SRC motif - Tyrosine-protein kinase Fyn (FYN) SH2 domain interaction


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

(2) Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins.
Sotgia et al. Biochemistry (2001)

See also

Other switches involving participants
Dystroglycan (DAG1) - 3 more (view)
Tyrosine-protein kinase Fyn (FYN) - 1 more (view)
Dystrophin (DMD) - 2 more (view)

Other switches involving interfaces
SH2 domain - 140 more (view)
WW domain - 105 more (view)
LIG_SH2_SRC - 8 more (view)
LIG_WW_1 - 17 more (view)

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