期刊
FEBS LETTERS
卷 583, 期 22, 页码 3563-3568出版社
WILEY
DOI: 10.1016/j.febslet.2009.10.060
关键词
Carbonic anhydrase IX; pH regulation, Cell adhesion; Ectodomain shedding; Hypoxia; Acidosis
资金
- Research and Development Support Agency [APVV-51-024805]
- EU
Carbonic anhydrase IX (CA IX) is a tumor-associated, hypoxia-induced enzyme involved in pH regulation and cell adhesion. Its catalytically active ectodomain (ECD) is linked to a transmembrane region and a short intracellular (IC) tail. Removal of the IC tail causes intracellular localization of CA IX. Mutations of basic amino acids within IC do not perturb the membrane position, but reduce shedding of the CA IX ectodomain as well as CA IX-mediated cell dissociation. Moreover, they abolish the CA IX capacity to acidify extracellular pH (pHe) and bind CA IX-selective sulfonamide inhibitor in hypoxia. These findings provide the first evidence for the critical contribution of the IC tail to the proper functioning of CA IX. Structured summary: MINT-7293982: E-cadherin (uniprotkb:Q95LE0) and CA IX (genbank_protein_gi:223556027) colocalize (MI:0403) by fluorescence microscopy (MI:0416) (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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