Mutational analysis of uncharged polar residues and proline in the distal one-third (Thr130-Pro142) of the highly conserved region of mouse Slc10a2

Solute carrier family member 2 (SLC10A2) reabsorbs bile acids at the distal terminus of the ileum in an Na + -dependent manner. Alignment of deduced amino acid sequences of SLC10 family members and homologous genes in various species revealed a highly conserved region that corresponds to Gly 104 -Pr...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2009-07, Vol.73 (7), p.1535-1540
Main Authors: Saeki, T.(Kyoto Prefectural Univ. (Japan)), Mizushima, S, Ueda, K, Iwami, K, Kanamoto, R
Format: Article
Language:English
Subjects:
ACIDE BILIAIRE
ACIDOS BILIARES
Amino Acid Sequence
AMINO ACID SEQUENCES
Animals
bile acid
BILE ACIDS
Biological and medical sciences
Cell Line
cell-surface biotinylation
Conserved Sequence - genetics
dependent transporter
DNA Mutational Analysis
Fundamental and applied biological sciences. Psychology
Humans
INTESTIN
INTESTINES
INTESTINOS
MICE
Molecular Sequence Data
MUTACION
MUTATION
Organic Anion Transporters, Sodium-Dependent - chemistry
Organic Anion Transporters, Sodium-Dependent - genetics
Organic Anion Transporters, Sodium-Dependent - metabolism
PROLINA
PROLINE
Proline - genetics
Protein Transport
Rabbits
RATON
SECUENCIAS DE AMINOACIDOS
Sequence Alignment
SEQUENCE D'ACIDES AMINES
site-directed mutagenesis
SOURIS
Symporters - chemistry
Symporters - genetics
Symporters - metabolism
Taurocholic Acid - metabolism
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Summary:Solute carrier family member 2 (SLC10A2) reabsorbs bile acids at the distal terminus of the ileum in an Na + -dependent manner. Alignment of deduced amino acid sequences of SLC10 family members and homologous genes in various species revealed a highly conserved region that corresponds to Gly 104 -Pro 142 of SLC10A2. To elucidate the functional importance of this region, uncharged polar residues and Pro in the distal one-third of this region in mouse Slc10a2 (mSlc10a2) were submitted to mutational analysis, and taurocholic acid uptake and cell surface localization were evaluated. In addition to mutations that abolished almost all of the transport activity with and without cellular localization failure (P142V and T130A respectively), a mutation that perhaps affected affinity for taurocholic acid was identified (T134A). These results suggest that the highly conserved region contains residues involved in the substrate interaction, function, and cellular localization of mSlc10a2.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.90023