ABCMdb

ABCC7 p.Leu1480Val

None has been submitted yet.

Publications

PMID: 11158634 [PubMed] Raghuram V et al: "Regulation of cystic fibrosis transmembrane conductance regulator single-channel gating by bivalent PDZ-domain-mediated interaction."

No. Sentence Comment

110 The mutation L1480A resulted in a complete loss of interaction, and mutations T1378A, L1480V, and L1480M resulted in markedly reduced interaction (Fig. 1D), with both PDZ1 and PDZ2 having similar specificities for their target ligands. Login to comment

PMID: 17392477 [PubMed] Wendeler MW et al: "Improved maturation of CFTR by an ER export signal."

No. Sentence Comment

36 Substitution of the most C-terminal leucine at position 1480 by valine was carried out by QuikChange mutagenesis (Stratagene, San Diego, CA, USA) using complementary oligonucleotides for changing codon CTT to GTT. Login to comment
86 The wild-type tail and the modified tail with L1480V mutation (underlined) are shown. Login to comment
87 B) HEK293 cells stably expressing wild-type or L1480V mutated CFTR constructs were pulse-labeled with [35 S]methionine for 20 min, chased for the indicated times, and subjected to immunoprecipitation with anti-CFTR antibodies. Login to comment
91 Values of CFTR with C) wild-type tail (HEK clone 6) and D) L1480V modified tail (HEK293 clone 1). Login to comment
127 A) HEK293 cells stably expressing wild-type or L1480V mutated CFTR constructs were pulse-labeled with [35 S]methionine, chased for the indicated times, and subjected to immunoprecipitation with anti-CFTR antibodies. Immunoprecipitates were then separated by SDS-PAGE and visualized by fluorography. Note that only the complex glycosylated mature form (band C) of CFTR constructs is detected. B) Quantification of fluorograms as shown in panel A. Login to comment
128 Black data points indicate the complex glycosylated form of wild-type CFTR and white data points the complex glycosylated form of the CFTR L1480V mutation. Login to comment
131 The L1480V substitution not only needs to be discussed in the context of ER export but also because L1480 is part of a PDZ binding motif. Login to comment
136 The substitution of leucine 1480 by a valine reported here, however, is a conservative mutation not expected to interfere with PDZ binding, since it meets the PDZ type I consensus sequence S/T-X-V/ I/L/F/Y (43). Login to comment
137 Accordingly, protein labeling of intact adherent cells by a membrane-impermeable biotinylation reagent showed that the L1480V substitution did not interfere with surface localization of mature CFTR (Fig. 2). Login to comment
163 However, our results showed that the L1480V substitution on CFTR-⌬F508 was not able to overcome the retention of misfolded molecules. Login to comment

PMID: 11597353 [PubMed] Boucherot A et al: "Role of CFTR's PDZ1-binding domain, NBF1 and Cl(-) conductance in inhibition of epithelial Na(+) channels in Xenopus oocytes."

No. Sentence Comment

63 The C-terminal PDZ-BD of CFTR is not required for activation of CFTR or inhibition of ENaC in Xenopus oocytes The PDZ-BD at the C-terminal end of CFTR was mutated in vitro (L1480V-CFTR) and coexpressed together with the epithelial NaW channel in Xenopus oocytes. Login to comment
67 A Cl3 conductance (GCFTR) of similar magnitude was activated in both wtCFTR and L1480V-CFTR expressing oocytes upon stimulation with IBMX and forskolin (I/F). Login to comment
74 Original recordings of the whole cell currents measured in a Xenopus oocyte coexpressing L1480V-CFTR and ENaC. Login to comment
91 Coexpression of wtCFTR, L1480V-CFTR, E831X-CFTR and E1474X with ENaC. Login to comment
94 Stimulation of either wtCFTR, L1480V-CFTR, E831X-CFTR or E1474X signi'cantly enhanced CFTR whole cell Cl3 conductance. Login to comment
150 Although the L1480V-CFTR mutant allows only marginal binding of NHERF to CFTR [12], activation of L1480V-CFTR by IBMX and forskolin was comparable to that of wtCFTR and even the N-terminal half of CFTR (E831X) was still partially activated by increase in intracellular cAMP. Login to comment