ABCMdb

PMID: 24178769

Cesaro L, Marin O, Venerando A, Donella-Deana A, Pinna LA
Phosphorylation of cystic fibrosis transmembrane conductance regulator (CFTR) serine-511 by the combined action of tyrosine kinases and CK2: the implication of tyrosine-512 and phenylalanine-508.
Amino Acids. 2013 Dec;45(6):1423-9. doi: 10.1007/s00726-013-1613-y. Epub 2013 Nov 1., [PubMed]

Sentences

No. Mutations Sentence Comment

49 ABCC7 p.Tyr512Ala As shown in Table 1 neither the parent peptide nor any of the substituted peptides were significantly phosphorylated by CK2, with the notable exception of the peptide in which Tyr512 was replaced by alanine (peptide 4). Login to comment 51 ABCC7 p.Tyr512Phe ABCC7 p.Tyr512Asp To note that phosphorylation is not restored if Tyr512 is replaced by Phe instead of Ala (peptide 8), while it is dramatically enhanced if Tyr512 is replaced by aspartic acid (peptide 9). Login to comment 105 ABCC7 p.Tyr512Ala ABCC7 p.Tyr512Ala Peptides reproducing the 500-523 sequence of F508delCFTR were synthesized either as such (see legend of Fig. 2) or with Tyr512 replaced by Ala (Y512A) or by phospho-tyrosine (pY512). Login to comment 108 ABCC7 p.Tyr512Ala Lanes 1, 2 and 3 refer to unsubstituted, Y512A and pY512 peptides, respectively. Login to comment 119 ABCC7 p.Tyr512Ala The mechanism of Ser511 phosphorylation outlined here can also provide an explanation for the finding that two CFTR mutants, in which Tyr512 has been replaced by Ala and Asp, respectively, undergo defective maturation with reduced cell surface exposition (Luz et al. 2011). Login to comment