ABCMdb

PMID: 12615054

Hegedus T, Sessler T, Scott R, Thelin W, Bakos E, Varadi A, Szabo K, Homolya L, Milgram SL, Sarkadi B
C-terminal phosphorylation of MRP2 modulates its interaction with PDZ proteins.
Biochem Biophys Res Commun. 2003 Mar 14;302(3):454-61., [PubMed]

Sentences

No. Mutations Sentence Comment

38 ABCC2 p.Ser1542Ala ABCC2 p.Ser1542Glu The binding of EBP50 and IKEPP was studied to mutant MRP2 variants (S1542A and S1542E), mimicking the non-phosphorylated and the phosphorylated serine, respectively. Login to comment 39 ABCC2 p.Ser1542Ala ABCC2 p.Ser1542Glu The binding of EBP50 and IKEPP was studied to mutant MRP2 variants (S1542A and S1542E), mimicking the non-phosphorylated and the phosphorylated serine, respectively. Login to comment 104 ABCC2 p.Ser1542Ala ABCC2 p.Ser1542Glu In order to investigate the role of this residue in PDZ interactions, the serine was replaced either by alanine (MRP2 S1542A) or by glutamic acid (MRP2 S1542E). Login to comment 105 ABCC2 p.Ser1542Ala ABCC2 p.Ser1542Glu MRP2 S1542A mimicked the dephosphorylated, while MRP2 S1542E the phosphorylated states of the PDZ binding motif. Login to comment 106 ABCC2 p.Ser1542Ala ABCC2 p.Ser1542Glu In order to investigate the role of this residue in PDZ interactions, the serine was replaced either by alanine (MRP2 S1542A) or by glutamic acid (MRP2 S1542E). Login to comment 107 ABCC2 p.Ser1542Ala ABCC2 p.Ser1542Ala ABCC2 p.Ser1542Glu ABCC2 p.Ser1542Glu The MRP2 S1542E mutant interacted with EBP50 much stronger than the wild type MRP2, whereas the MRP2 S1542A variant showed less EBP50 binding compared to the wild type MRP2. Login to comment 109 ABCC2 p.Ser1542Ala ABCC2 p.Ser1542Glu ABCC2 p.Ser1542Glu The autoradiogram shown in Fig. 3B reveals that the MRP2 S1542E mutant bound IKEPP much more efficiently than the wild type MRP2. Login to comment 111 ABCC2 p.Ser1542Glu The autoradiogram shown in Fig. 3B reveals that the MRP2 S1542E mutant bound IKEPP much more efficiently than the wild type MRP2. Login to comment 116 ABCC2 p.Ser1542Glu We found that the interaction of IKEPP with the MRP2 S1542E mutant was stronger in the full concentration range, as Table 1 Summary of the overlay experiments PDZ/ABC proteins MRP2 CFTR ABCA1 PDZK1 +* +* ) IKEPP + + ) EBP50 + + ) E3KARP ) + ) SAP-97 ) ) ) b2-syntrophin ) ) + Interacting pairs of ABC and PDZ proteins are labeled as ''+``, whereas '')`` represents the pairs which exhibited no binding in our overlay experiments. Login to comment 118 ABCC2 p.Ser1542Glu We found that the interaction of IKEPP with the MRP2 S1542E mutant was stronger in the full concentration range, as Table 1 Summary of the overlay experiments PDZ/ABC proteins MRP2 CFTR ABCA1 PDZK1 +* +* ) IKEPP + + ) EBP50 + + ) E3KARP ) + ) SAP-97 ) ) ) b2-syntrophin ) ) + Interacting pairs of ABC and PDZ proteins are labeled as ''+``, whereas '')`` represents the pairs which exhibited no binding in our overlay experiments. Login to comment 119 ABCC2 p.Ser1542Ala However, the binding of IKEPP to the MRP2 S1542A mutant was found to be similar to the interaction with the wild type. Login to comment 121 ABCC2 p.Ser1542Ala ABCC2 p.Ser1542Glu Similar experiments with EBP50 showed a preferential binding of this PDZ protein to MRP2 S1542E at various EBP50 concentrations (data not shown). Login to comment 123 ABCC2 p.Ser1542Glu Similar experiments with EBP50 showed a preferential binding of this PDZ protein to MRP2 S1542E at various EBP50 concentrations (data not shown). Login to comment 141 ABCC2 p.Ser1542Ala ABCC2 p.Ser1542Glu Wild type (WT), mutants mimicking the phosphorylated (S1542E) and dephosphorylated (S1542A) states of PDZ binding motif, and a variant containing glycines in place of the last four, C-terminal amino acids (4G), were studied. Login to comment 143 ABCC2 p.Ser1542Ala ABCC2 p.Ser1542Glu Wild type (WT), mutants mimicking the phosphorylated (S1542E) and dephosphorylated (S1542A) states of PDZ binding motif, and a variant containing glycines in place of the last four, C-terminal amino acids (4G), were studied. Login to comment 162 ABCC2 p.Ser1542Glu The binding of the phosphorylation mimicking MRP2 S1542E mutant and the phosphorylated C-terminal peptide to EBP50 changed in our experiments. Login to comment 164 ABCC2 p.Ser1542Glu The binding of the phosphorylation mimicking MRP2 S1542E mutant and the phosphorylated C-terminal peptide to EBP50 changed in our experiments. Login to comment