ABCMdb

ABCG2 p.Gly553Glu

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Publications

PMID: 16618113 [PubMed] Polgar O et al: "Mutational studies of G553 in TM5 of ABCG2: a residue potentially involved in dimerization."

No. Sentence Comment

7 Similar results were observed with the G553E mutant. Login to comment
9 Despite its altered localization, the G553L and G553E mutants were cross-linked using amine-reactive cross-linkers with multiple arm lengths, suggesting that the monomers are in the proximity of each other but are unable to complete normal trafficking. Login to comment
48 The G553L and G553E mutants were generated by site-directed mutagenesis in the pcDNA3.1/ Myc-HisA(-) vector (Invitrogen) as previously described (23). Login to comment
162 Evaluating the effect of a charged residue at position 553, we replaced the glycine with glutamic acid (G553E) and transfected HEK 293 cells. Login to comment
164 Figure 9 shows that, like the leucine mutant, the G553E mutant did not move to the cell surface as verified by no staining with the 5D3 surface antibody on flow cytometry (Figure 9A). Login to comment
166 The G553E mutant, like the G553L mutant, is represented by a double band on immunoblots, suggestive of impaired glycosylation, and in fact, following treatment with PNGase F, only one lower-molecular mass band was visible upon immunoblotting (data not shown). Login to comment
169 We found that substitution of glycine 553 with either leucine (G553L) or glutamic acid (G553E) followed by transfection into HEK 293 cells resulted in a markedly reduced level of protein expression with impaired glycosylation and predominant ER retention. Login to comment
192 In addition to the above-mentioned aberrant localization in the mammalian cells, the glycosylation pattern of the G553L and G553E mutants was also altered. Login to comment
210 FIGURE 9: Surface expression of the G553E mutant in HEK 293 cells and cross-linking with DSG. Login to comment
211 (A) The G553E mutant (six clones are shown) is not detectable on the cell surface with the 5D3 antibody by flow cytometry performed as described in the legend of Figure 2: negative control antibody (s) or 5D3 antibody (- - -). Login to comment
212 (B) Cross-linking (as detailed in Figure 5) is observed following treatment of transfected HEK 293 cells with DSG in case of both the wild type (50 µg of protein) and the G553E mutant (100 µg of protein). Login to comment
228 The G589E mutation in the white protein, analogous to our ABCG2 G553E mutant, apparently disrupts the white-brown heterodimer as suggested by the significantly reduced red eye pigment levels. Login to comment

PMID: 17027309 [PubMed] Li YF et al: "Towards understanding the mechanism of action of the multidrug resistance-linked half-ABC transporter ABCG2: a molecular modeling study."

No. Sentence Comment

179 T mutant binds more tightly to Rhodamin123 and inhibits rhodamine123 transport [19,51,21] G553L, G553E TM5 In drosophila, mutation at this position yields monomer. Login to comment
244 Introducing a larger or charged residue at this position (G553L and G553E) would result in a clash of amino acid side chains and disrupt the dimer formation both in ABCG2 and in its Drosophila orthologue. Login to comment

PMID: 18249138 [PubMed] Hazai E et al: "Homology modeling of breast cancer resistance protein (ABCG2)."

No. Sentence Comment

245 However, in our model, R482 cannot form interaction with rhodamine, but L484 is in interacting distance Table 3 Mutations on BCRP and their effect on its function Mutation Effect/results Reference V12M Did not effect Hemato and MTX transport Tamura et al. (2006) G51C Did not effect Hemato and MTX transport Tamura et al. (2006) K86M Inactivates transporter (dominant negative effect on ATPase activity); alters subcellular distribution Henriksen et al. (2005a) K86M Transporter inactive, but still able to bind ATP Ozvegy et al. (2002) Q126stop Defective porphyrin transport Tamura et al. (2006) Q141K Did not effect Hemato and MTX transport Tamura et al. (2006) T153M Did not effect Hemato and MTX transport Tamura et al. (2006) Q166E Did not effect Hemato and MTX transport Tamura et al. (2006) I206L Did not effect Hemato and MTX transport Tamura et al. (2006) F208S Defective porphyrin transport Tamura et al. (2006) S248P Defective porphyrin transport Tamura et al. (2006) E334stop Defective porphyrin transport Tamura et al. (2006) F431L Effects MTX transport Tamura et al. (2006) S441N Defective porphyrin transport Tamura et al. (2006) E446-mutants No drug resistance Miwa et al. (2003) R482G, R482T Effects MTX transport Tamura et al. (2006) R482T Substrate drug transport and inhibitor efficiency is not mediated by changes in drug-binding Pozza et al. (2006) R482G, R482T Substitution influence the substrate specificity of the transporter Ozvegy et al. (2002) R482G, R482T Altered substrate specificity Honjo et al. (2001) R482G Methotrexate not transported Chen et al. (2003b) Mitomo et al. (2003) R482G Resistance to hydrophilic antifolates in vitro, G482-ABCG2 mutation confers high-level resistance to various hydrophilic antifolates Shafran et al., (2005) R482G Three distinct drug, binding sites Clark et al. (2006) R482G Altered substrate specificity, granulocyte maturation uneffected Ujhelly et al. (2003) R482 mutants Higher resistance to mitoxantrone and doxorubicin than wt Miwa et al. (2003) R482X Affects substrate transport and ATP hydrolysis but not substrate binding Ejendal et al. (2006) F489L Impaired porphyrin transport Tamura et al. (2006) G553L; G553E Impaired trafficing, expression, and N-linked glycosylation Polgar et al. (2006) L554P Dominant negative effect on drug sensitivity Kage et al. (2002) N557D Resistance to MTX, but decreased transport of SN-38; N557E no change in transport compared to wt Miwa et al. (2003) F571I Did not effect Hemato and MTX transport Tamura et al. (2006) N590Y Did not effect Hemato and MTX transport Tamura et al. (2006) C592A Impaired function and expression Henriksen et al. (2005b) C592A/C608A Restored plasma mb expression; MTX transport normal, BODIPY-prazosin impaired Henriksen et al. (2005b) C603A Disulfide bridge; no functional or membrane targeting change Henriksen et al. (2005b) C608A Impaired function and expression Henriksen et al. (2005b) D620N Did not effect Hemato and MTX transport Tamura et al. (2006) H630X No change in transport Miwa et al. (2003) Cand N-terminal truncated Impaired trafficing Takada et al. (2005) with the ligand. Login to comment

PMID: 20812902 [PubMed] Ni Z et al: "Structure and function of the human breast cancer resistance protein (BCRP/ABCG2)."

No. Sentence Comment

293 Leu or Glu substitution of Gly553 led to rapid degradation and retention in the endoplasm reticulum of BCRP [130], suggesting that Gly553 is critical for plasma membrane targeting and proper folding of the transporter. Login to comment

PMID: 21184741 [PubMed] Sugiyama T et al: "Posttranslational negative regulation of glycosylated and non-glycosylated BCRP expression by Derlin-1."

No. Sentence Comment

163 Further, we could also assess the impact of Der- lin-1 on the expression of other BCRP variants such as R383A, G553L and G553E variants, which are also shown to be impaired N-linked glycosylation like N596Q BCRP [27,28]. Login to comment