Membrane-anchored carbonic anhydrase IV interacts with monocarboxylate transporters via their chaperones CD147 and GP70.
Amino Acid Sequence
Animals
Basigin
/ chemistry
Carbonic Anhydrase IV
/ metabolism
Glycoproteins
/ metabolism
HEK293 Cells
Humans
Membrane Glycoproteins
/ metabolism
Membrane Proteins
Models, Molecular
Molecular Chaperones
/ metabolism
Monocarboxylic Acid Transporters
/ metabolism
Protein Domains
Protein Interaction Maps
Rats
Sequence Alignment
Symporters
/ metabolism
Xenopus
Xenopus
electrophysiology
energy metabolism
ion-sensitive electrode
lactic acid
membrane transport
pH regulation
protein complex
protein expression
proton transport
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
11 01 2019
11 01 2019
Historique:
received:
24
08
2018
revised:
12
11
2018
pubmed:
18
11
2018
medline:
6
5
2019
entrez:
18
11
2018
Statut:
ppublish
Résumé
Monocarboxylate transporters (MCTs) mediate the proton-coupled exchange of high-energy metabolites, including lactate and pyruvate, between cells and tissues. The transport activity of MCT1, MCT2, and MCT4 can be facilitated by the extracellular carbonic anhydrase IV (CAIV) via a noncatalytic mechanism. Combining physiological measurements in HEK-293 cells and
Identifiants
pubmed: 30446621
pii: S0021-9258(20)40374-6
doi: 10.1074/jbc.RA118.005536
pmc: PMC6333884
doi:
Substances chimiques
EMB protein, human
0
Emb protein, rat
0
Glycoproteins
0
Membrane Glycoproteins
0
Membrane Proteins
0
Molecular Chaperones
0
Monocarboxylic Acid Transporters
0
Slc16a7 protein, rat
0
Symporters
0
monocarboxylate transport protein 1
0
Basigin
136894-56-9
Carbonic Anhydrase IV
EC 4.2.1.-
Banques de données
PDB
['5JN9', '3B5H']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
593-607Informations de copyright
© 2019 Forero-Quintero et al.
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