ABCG2 p.Arg383Lys
[switch to full view]Comments [show]
None has been submitted yet.
No.
Sentence
Comment
41
Mutagenesis and transfection The R383A, R383G, R383H, R383K, and R383G/S384R mutants were generated by site-directed mutagenesis in the pcDNA3.1/Myc-HisA(-) vector (Invitrogen) as previously described [26].
X
ABCG2 p.Arg383Lys 19406100:41:54
status: VERIFIED183 We postulated that this arginine might function as an anchor of the first transmembrane alpha helix, thus more conservative substitutions were performed: mutation to the positively charged lysine and introduction of arginine at position 384 instead of 383, creating the R383K and R383G/S384R mutants, followed by stable transfections in HEK 293 cells.
X
ABCG2 p.Arg383Lys 19406100:183:270
status: VERIFIED184 Like R383A, the R383K mutant displayed some surface expression on flow cytometry (Fig. 7A) and the protein was detectable on immunoblot, though expression levels were still markedly reduced when compared to the wild-type transfectant (Fig. 7B).
X
ABCG2 p.Arg383Lys 19406100:184:16
status: VERIFIED185 Just as observed for the alanine mutant, R383K was represented by a double band on immunoblot suggestive of altered glycosylation.
X
ABCG2 p.Arg383Lys 19406100:185:41
status: VERIFIED187 Surface expression, function and protein levels of the R383K mutant transfected into HEK 293 cells.
X
ABCG2 p.Arg383Lys 19406100:187:55
status: VERIFIED188 (A) The R383K mutant (clone #8) detected on the cell surface with the 5D3 antibody by flow cytometry performed as described for Fig. 2.
X
ABCG2 p.Arg383Lys 19406100:188:8
status: VERIFIED193 functionality of the R383K mutant was also assessed in flow cytometry-based transport assays.
X
ABCG2 p.Arg383Lys 19406100:193:21
status: VERIFIED256 The R383K mutant, which preserved the strong positive charge at this position, was detectable on the cell surface and transported the tested substrates, though protein expression levels were significantly reduced.
X
ABCG2 p.Arg383Lys 19406100:256:4
status: VERIFIED