ABCMdb

ABCC2 p.Ser1542Glu

None has been submitted yet.

Publications

PMID: 12615054 [PubMed] Hegedus T et al: "C-terminal phosphorylation of MRP2 modulates its interaction with PDZ proteins."

No. Sentence Comment

38 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 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 MRP2 S1542A mimicked the dephosphorylated, while MRP2 S1542E the phosphorylated states of the PDZ binding motif. Login to comment
107 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 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 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
121 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 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 The binding of the phosphorylation mimicking MRP2 S1542E mutant and the phosphorylated C-terminal peptide to EBP50 changed in our experiments. Login to comment
39 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
106 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
111 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
118 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
123 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
143 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
164 The binding of the phosphorylation mimicking MRP2 S1542E mutant and the phosphorylated C-terminal peptide to EBP50 changed in our experiments. Login to comment