ABCC2 p.Ser1542Ala
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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.
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ABCC2 p.Ser1542Ala 12615054:38:68
status: NEW104 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).
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ABCC2 p.Ser1542Ala 12615054:104:118
status: NEW105 MRP2 S1542A mimicked the dephosphorylated, while MRP2 S1542E the phosphorylated states of the PDZ binding motif.
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ABCC2 p.Ser1542Ala 12615054:105:5
status: NEW107 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.
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ABCC2 p.Ser1542Ala 12615054:107:5
status: NEWX
ABCC2 p.Ser1542Ala 12615054:107:101
status: NEW109 The autoradiogram shown in Fig. 3B reveals that the MRP2 S1542E mutant bound IKEPP much more efficiently than the wild type MRP2.
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ABCC2 p.Ser1542Ala 12615054:109:101
status: NEW119 However, the binding of IKEPP to the MRP2 S1542A mutant was found to be similar to the interaction with the wild type.
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ABCC2 p.Ser1542Ala 12615054:119:42
status: NEW121 Similar experiments with EBP50 showed a preferential binding of this PDZ protein to MRP2 S1542E at various EBP50 concentrations (data not shown).
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ABCC2 p.Ser1542Ala 12615054:121:42
status: NEW141 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.
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ABCC2 p.Ser1542Ala 12615054:141:84
status: NEW39 The binding of EBP50 and IKEPP was studied to mutant MRP2 variants (S1542A and S1542E), mimicking the non-phosphorylated and the phosphorylated serine, respectively.
X
ABCC2 p.Ser1542Ala 12615054:39:68
status: NEW106 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).
X
ABCC2 p.Ser1542Ala 12615054:106:118
status: NEW143 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.
X
ABCC2 p.Ser1542Ala 12615054:143:84
status: NEW
PMID: 11274200
[PubMed]
Harris MJ et al: "Identification of the apical membrane-targeting signal of the multidrug resistance-associated protein 2 (MRP2/MOAT)."
No.
Sentence
Comment
115
E, S1542A, mutation of the serine produced a less distinct distribution.
X
ABCC2 p.Ser1542Ala 11274200:115:3
status: NEW