ABCA1 p.Thr1243Ala
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PMID: 15218032
[PubMed]
Roosbeek S et al: "Phosphorylation by protein kinase CK2 modulates the activity of the ATP binding cassette A1 transporter."
No.
Sentence
Comment
94
Similar measurements were performed in the presence of 50 M 4,5,6,7-tetrabromobenzotriazole and apigenin CK2 inhibitors on Mock-transfected and Hek-293 cells transfected with WT ABCA1 and with the T1242A, T1243A, T1242A/T1243A, and T1242D/T1243D ABCA1 mutants.
X
ABCA1 p.Thr1243Ala 15218032:94:213
status: NEWX
ABCA1 p.Thr1243Ala 15218032:94:228
status: NEW133 In both systems we engineered several mutants designed at preventing phosphorylation by mutation either of the target threonines and serine, T1242A, T1243A, T1242A/ T1243A, S1255A, or of the downstream cluster of acidic residues, E1245Q, E1246Q, E1245Q/E1246Q.
X
ABCA1 p.Thr1243Ala 15218032:133:149
status: NEWX
ABCA1 p.Thr1243Ala 15218032:133:165
status: NEW143 Analysis of the T1242A, T1243A, and T1242A/T1243A NBD1 mutants supports the loss of either one or two threonine phosphorylation sites in the mutated peptides, whereas the Ser-1255 site is preserved.
X
ABCA1 p.Thr1243Ala 15218032:143:24
status: NEWX
ABCA1 p.Thr1243Ala 15218032:143:43
status: NEW159 Compared with WT ABCA1, set as 100%, the PE and PS content in the outer leaflet of the plasma membrane increased up to 130 Ϯ 14 and 123 Ϯ 8% for the T1242A mutant, 154 Ϯ 15 and 148 Ϯ 11% for the T1243A mutant, 170 Ϯ 15 and 207 Ϯ 16% for the T1242A/T1243A mutant, 141 Ϯ 11 and 136 Ϯ 10% for the S1255A mutant, and 141 Ϯ 13 and 120 Ϯ 9% for the E1245Q/E1246Q mutant, respectively (Fig. 4).
X
ABCA1 p.Thr1243Ala 15218032:159:219
status: NEWX
ABCA1 p.Thr1243Ala 15218032:159:284
status: NEW162 The effect of the specific CK2 inhibitors 4,5,6,7-tetrabromo- benzotriazole and apigenin on the flippase activity in Hek-293 Tet-Off cells transfected with WT ABCA1 and with the T1242A, T1243A, T1242A/T1243A, S1255A, and T1242D/ T1243D mutants was consistent with the above data.
X
ABCA1 p.Thr1243Ala 15218032:162:186
status: NEWX
ABCA1 p.Thr1243Ala 15218032:162:201
status: NEW176 TABLE I Mass spectrometric analysis of NBD1ϩR1 phosphorylation NBD1ϩR1 Tryptic peptide Molecular mass Molecular mass after beta-elimination Phosphorylated residues Da Da WT Leu-1229-Arg-1269 4542.5 4249.5 Thr-1242, Thr-1243, Ser-1255 T1242A Leu-1229-Lys-1250 2483.6 2385.9 Thr-1243 T1242A Val-1251-Arg-1272 2411.6 2313.7 Ser-1255 T1243A Leu-1229-Lys-1250 2483.1 2385.2 Thr-1242 T1243A Val-1251-Arg-1272 2411.2 2313.2 Ser-1255 T1242A/T1243A Leu-1229-Lys-1250 2356.1 2356.1 T1242A/T1243A Val-1251-Arg-1272 2411.6 2313.7 Ser-1255 S1255A Val-1251-Arg-1272 2297.7 2297.7 compared with WT ABCA1.
X
ABCA1 p.Thr1243Ala 15218032:176:342
status: NEWX
ABCA1 p.Thr1243Ala 15218032:176:390
status: NEWX
ABCA1 p.Thr1243Ala 15218032:176:445
status: NEWX
ABCA1 p.Thr1243Ala 15218032:176:491
status: NEW177 This increase was more pronounced for the T1243A mutation either alone or in combination with the T1242A mutation, whereas the effect of the T1242A and S1255A mutants was similar.
X
ABCA1 p.Thr1243Ala 15218032:177:42
status: NEW188 The T1242A and T1243A mutations either alone or in combination and the E1245Q/ E1246Q mutation, which all decrease CK2 activity, increased phospholipid and cholesterol efflux (Fig. 7, A and B).
X
ABCA1 p.Thr1243Ala 15218032:188:15
status: NEW92 Similar measurements were performed in the presence of 50 òe;M 4,5,6,7-tetrabromobenzotriazole and apigenin CK2 inhibitors on Mock-transfected and Hek-293 cells transfected with WT ABCA1 and with the T1242A, T1243A, T1242A/T1243A, and T1242D/T1243D ABCA1 mutants.
X
ABCA1 p.Thr1243Ala 15218032:92:212
status: NEWX
ABCA1 p.Thr1243Ala 15218032:92:227
status: NEW131 In both systems we engineered several mutants designed at preventing phosphorylation by mutation either of the target threonines and serine, T1242A, T1243A, T1242A/ T1243A, S1255A, or of the downstream cluster of acidic residues, E1245Q, E1246Q, E1245Q/E1246Q.
X
ABCA1 p.Thr1243Ala 15218032:131:149
status: NEWX
ABCA1 p.Thr1243Ala 15218032:131:165
status: NEW141 Analysis of the T1242A, T1243A, and T1242A/T1243A NBD1 mutants supports the loss of either one or two threonine phosphorylation sites in the mutated peptides, whereas the Ser-1255 site is preserved.
X
ABCA1 p.Thr1243Ala 15218032:141:24
status: NEWX
ABCA1 p.Thr1243Ala 15218032:141:43
status: NEW157 Compared with WT ABCA1, set as 100%, the PE and PS content in the outer leaflet of the plasma membrane increased up to 130 afe; 14 and 123 afe; 8% for the T1242A mutant, 154 afe; 15 and 148 afe; 11% for the T1243A mutant, 170 afe; 15 and 207 afe; 16% for the T1242A/T1243A mutant, 141 afe; 11 and 136 afe; 10% for the S1255A mutant, and 141 afe; 13 and 120 afe; 9% for the E1245Q/E1246Q mutant, respectively (Fig. 4).
X
ABCA1 p.Thr1243Ala 15218032:157:219
status: NEWX
ABCA1 p.Thr1243Ala 15218032:157:284
status: NEW160 The effect of the specific CK2 inhibitors 4,5,6,7-tetrabromo- benzotriazole and apigenin on the flippase activity in Hek-293 Tet-Off cells transfected with WT ABCA1 and with the T1242A, T1243A, T1242A/T1243A, S1255A, and T1242D/ T1243D mutants was consistent with the above data.
X
ABCA1 p.Thr1243Ala 15218032:160:186
status: NEWX
ABCA1 p.Thr1243Ala 15218032:160:201
status: NEW174 TABLE I Mass spectrometric analysis of NBD1af9;R1 phosphorylation NBD1af9;R1 Tryptic peptide Molecular mass Molecular mass after beta-elimination Phosphorylated residues Da Da WT Leu-1229-Arg-1269 4542.5 4249.5 Thr-1242, Thr-1243, Ser-1255 T1242A Leu-1229-Lys-1250 2483.6 2385.9 Thr-1243 T1242A Val-1251-Arg-1272 2411.6 2313.7 Ser-1255 T1243A Leu-1229-Lys-1250 2483.1 2385.2 Thr-1242 T1243A Val-1251-Arg-1272 2411.2 2313.2 Ser-1255 T1242A/T1243A Leu-1229-Lys-1250 2356.1 2356.1 T1242A/T1243A Val-1251-Arg-1272 2411.6 2313.7 Ser-1255 S1255A Val-1251-Arg-1272 2297.7 2297.7 Protein Kinase CK2 Phosphorylation Modulates ABCA1 Activity compared with WT ABCA1.
X
ABCA1 p.Thr1243Ala 15218032:174:342
status: NEWX
ABCA1 p.Thr1243Ala 15218032:174:390
status: NEWX
ABCA1 p.Thr1243Ala 15218032:174:445
status: NEWX
ABCA1 p.Thr1243Ala 15218032:174:491
status: NEW175 This increase was more pronounced for the T1243A mutation either alone or in combination with the T1242A mutation, whereas the effect of the T1242A and S1255A mutants was similar.
X
ABCA1 p.Thr1243Ala 15218032:175:42
status: NEW186 The T1242A and T1243A mutations either alone or in combination and the E1245Q/ E1246Q mutation, which all decrease CK2 activity, increased phospholipid and cholesterol efflux (Fig. 7, A and B).
X
ABCA1 p.Thr1243Ala 15218032:186:15
status: NEW