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Alternative splicing removes the PDZ-binding motif of Guanine deaminase (GDA) (Nedasin), abrogating binding to Disks large homolog 3 (DLG3). Isoform 1 of Guanine deaminase (GDA) (Nedasin S) is predominately expressed in neuronal tissues and binds PDZ domains. Isoform 3 of Guanine deaminase (GDA) (Nedasin V1), which is predominately expressed in non-neuronal tissues, does not bind PDZ domains. The presence of Nedasin S inhibits binding of NMDA receptors and K+ channels to PDZ domain-containing proteins such as members of the MAGUK family. This suggests that GDA might modulate the receptor clustering function of the PDZ domains of MAGUK family members, and this modulation is regulated by alternative splicing of GDA transcripts.

(1) Guanine deaminase (GDA)
(2) Disks large homolog 3 (DLG3)

Interaction #1 GDA - DLG3

(1) LIG_PDZ_Class_1 motif (449PFSSSV454) in Guanine deaminase (GDA)
(2) PDZ domain (Also known as DHR or GLGF) (130-217) in Disks large homolog 3 (DLG3)

Interaction Regulation
Alternative splicing Abrogation of the Guanine deaminase (GDA) LIG_PDZ_Class_1 motif - Disks large homolog 3 (DLG3) PDZ domain (Also known as DHR or GLGF) interaction


(1) A novel NE-dlg/SAP102-associated protein, p51-nedasin, related to the amidohydrolase superfamily, interferes with the association between NE-dlg/SAP102 and N-methyl-D-aspartate receptor.
Kuwahara et al. J. Biol. Chem. (1999)

See also

Other switches involving participants
Disks large homolog 3 (DLG3) - 4 more (view)
Guanine deaminase (GDA) - 1 more (view)

Other switches involving interfaces
PDZ domain (Also known as DHR or GLGF) - 45 more (view)
LIG_PDZ_Class_1 - 41 more (view)

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