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Switch subtype:
Altered binding specificity

Adhesion-dependent phosphorylation of Y892 in Dystroglycan (DAG1) by c-Src (SRC) switches the specificity of DAG1 from WW domain containing proteins like Utrophin (UTRN) to SH2 domain containing proteins like Tyrosine-protein kinase CSK (CSK).

(1) Dystroglycan (DAG1)
(2) Utrophin (UTRN)
(3) Tyrosine-protein kinase CSK (CSK)

Interaction #1 DAG1 - UTRN

Is mutually exclusive with Interaction #2 DAG1 - CSK

(1) LIG_WW_1 motif (889PPPY892) in Dystroglycan (DAG1)
(2) WW domain (2815-2843) in Utrophin (UTRN)

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

Interaction #2 DAG1 - CSK

Is mutually exclusive with Interaction #1 DAG1 - UTRN

(3) LIG_SH2_SRC motif (892YVPP895) in Dystroglycan (DAG1)
(4) SH2 domain (82-156) in Tyrosine-protein kinase CSK (CSK)

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


(1) Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin.
James et al. J. Cell. Sci. (2000)

(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)

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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