ABCC7 p.Ser13Ala
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PMID: 17235394
[PubMed]
Thelin WR et al: "Direct interaction with filamins modulates the stability and plasma membrane expression of CFTR."
No.
Sentence
Comment
73
WT, S13F, and S13A CFTRs were transiently expressed in HEK293 cells, labeled, immunoprecipitated, and analyzed by autoradiography (Figure 2A).
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ABCC7 p.Ser13Ala 17235394:73:14
status: NEW75 After 4 hours of chase, WT and S13A CFTRs were present almost exclusively as the mature band C, while no band C was observed for ΔF508 (Figure 2B).
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ABCC7 p.Ser13Ala 17235394:75:31
status: NEW76 Like WT and S13A CFTR, S13F CFTR was clearly processed from the band B to band C protein during the first 4 hours of chase.
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ABCC7 p.Ser13Ala 17235394:76:12
status: NEW79 The half-life was similar between WT and S13A CFTR (22.5 and 22.6 hours, respectively; Figure 2C).
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ABCC7 p.Ser13Ala 17235394:79:41
status: NEW94 However, CFTR1-25/S13A peptides bound to FLNs similarly to the CFTR1-25 peptides (Figure 3B).
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ABCC7 p.Ser13Ala 17235394:94:18
status: NEW96 Thus, the reduction relative to WT CFTR in the band B/band C ratio observed for the S13F mutation, but not the S13A mutation, correlates with the ability to bind FLN-A in vitro.
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ABCC7 p.Ser13Ala 17235394:96:111
status: NEW101 Furthermore, FLN-A coprecipitated with WT and S13A CFTR expressed in HEK293 cells, but not with S13F CFTR (Figure 3E).
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ABCC7 p.Ser13Ala 17235394:101:46
status: NEW113 S13A, CFTR1-25/S13A.
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ABCC7 p.Ser13Ala 17235394:113:0
status: NEWX
ABCC7 p.Ser13Ala 17235394:113:15
status: NEW125 The surface pool of CFTR was detected by immunofluorescence in unpermeabilized baby hamster kidney (BHK) cells expressing either WT, S13A, S13F, or ΔF508 HA-CFTR.
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ABCC7 p.Ser13Ala 17235394:125:133
status: NEW126 We observed significant amounts of WT and S13A CFTR at the cell surface, while no signal was observed for ΔF508 (Figure 5A).
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ABCC7 p.Ser13Ala 17235394:126:42
status: NEW128 Unlike ΔF508 CFTR, we observed surface staining for S13F CFTR; however, the staining was greatly reduced compared with WT and S13A CFTR.
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ABCC7 p.Ser13Ala 17235394:128:132
status: NEW130 In agreement with our observations by immunofluorescence, a substantial pool of WT and S13A CFTR resided on the cell surface (41.2% and 37.8%, respectively), while no ΔF508 was observed (Figure 5B).
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ABCC7 p.Ser13Ala 17235394:130:87
status: NEW207 Additionally, S13F was prematurely sorted to lysosomes, which may explain why mature S13F CFTR was degraded more rapidly than the WT protein. Therefore, we examined the half-life of WT, S13F, and S13A CFTR by pulse chase in the presence of the lysosomal protease inhibitor leupeptin.
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ABCC7 p.Ser13Ala 17235394:207:196
status: NEW324 WT, S13F, S13A, and ΔF508 CFTRs were transiently expressed in HEK293 cells.
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ABCC7 p.Ser13Ala 17235394:324:10
status: NEW
PMID: 22874563
[PubMed]
Luciani A et al: "Targeting autophagy as a novel strategy for facilitating the therapeutic action of potentiators on DeltaF508 cystic fibrosis transmembrane conductance regulator."
No.
Sentence
Comment
108
We found that Vrx-770 was effective in stimulating the response to Fsk only when brushed nasal epithelial cells were pretreated with cystamine or EUK-134 (Fig. S13A).
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ABCC7 p.Ser13Ala 22874563:108:160
status: NEW111 We found that Vrx-770 was effective in stimulating the response to Fsk only when brushed nasal epithelial cells were pretreated with cystamine or EUK-134 (Fig. S13A).
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ABCC7 p.Ser13Ala 22874563:111:160
status: NEW