Molecular Mechanisms of Subcellular Localization of ABCG5 and ABCG8
スポンサーリンク
概要
- 論文の詳細を見る
Human ABCG subfamily proteins ABCG1, ABCG2, ABCG4, ABCG5, and ABCG8 are half-type ATP-binding cassette (ABC) proteins that transport sterols or xenobiotics. ABCG1, ABCG2, and ABCG4 function as homodimers on the plasma membrane. In contrast, ABCG5 and ABCG8 function as heterodimers on the plasma membrane, and the homodimer of either ABCG5 or ABCG8 is retained in the endoplasmic reticulum (ER). To examine the molecular mechanisms of the regulated trafficking of ABCG5 and ABCG8, the subcellular localizations of chimeric proteins, fused with ABCG1 or ABCG2, were analyzed. Homodimers of chimeric proteins, in which the N-terminal cytosolic domain of ABCG1 or ABCG2 was fused to the C-terminal transmembrane domain of ABCG5 or ABCG8 localized to the plasma membrane, whereas chimeric proteins in which the N-terminal cytosolic domain of ABCG5 or ABCG8 was fused to the C-terminal transmembrane domain of ABCG1 or ABCG2 localized to the ER. Mutations in ER-retrieval motif-like sequences in ABCG5 or ABCG8 did not affect their subcellular localization. This suggests that the N-terminal cytosolic domains of ABCG5 and ABCG8 are involved in ER retention of their homodimers, and that novel ER-retention or -retrieval motifs exist within these domains.
- 社団法人 日本農芸化学会の論文
著者
-
Ueda Kazumitsu
Laboratory Of Cellular Biochemistry Division Of Applied Life Sciences Graduate School Of Agriculture
-
Matsuo Michinori
Laboratory Of Cellular Biochemistry Division Of Applied Life Sciences Graduate School Of Agriculture
-
HIRATA Takashi
Laboratory of Cellular Biochemistry, Division of Applied Life Sciences, Kyoto University Graduate Sc
-
OKABE Morio
Laboratory of Cellular Biochemistry, Division of Applied Life Sciences, Kyoto University Graduate Sc
-
KOBAYASHI Aya
Laboratory of Cellular Biochemistry, Division of Applied Life Sciences, Kyoto University Graduate Sc
関連論文
- Detection of ABCA7-positive cells in salivary glands from patients with Sjogren's syndrome
- Mechanism of multidrug recognition by MDR1/ABCB1
- ABC proteins : key molecules for lipid homeostasis
- Inhibitory Effects of a Cyclosporin Derivative, SDZ PSC 833, on Transport of Doxorubicin and Vinblastine via Human P-Glycoprotein
- Application of Vanadate-Induced Nucleotide Trapping to Plant Cells for Detection of ABC Proteins
- Vinexin, CAP/ponsin, ArgBP2 : a Novel Adaptor Protein Family Regulating Cytoskeletal Organization and Signal Transduction
- Molecular Mechanisms of Subcellular Localization of ABCG5 and ABCG8
- Expression of Human P-Glycoprotein in Yeast Cells : Effects of Membrane Component Sterols on the Activity of P-Glycoprotein(Biological Chemistry)
- Production of a Site Specifically Cleavable P-Glycoprotein-β-galactosidase Fusion Protein(Biological Chemistry)
- The Effects of Metal Ions on the DNA Damage Induced by Hydrogen Peroxide(Biological Chemistry)
- Alternative Secondary Structures in the Phage G4 Origin of the Complementary DNA Strand Synthesis : Effects of NaCl Concentration on the Bleomycin-DNA Interaction
- Volume-Sensitive Cl^- Channel in Human Epithelial Cells : Regulation by ATP and Relation to P-Glycoprotein
- Human MDR1 and MRP1 Recognize Berberine as Their Transport Substrate
- Human MDR1 and MRP1 Recognize Berberine as Their Transport Substrate
- Molecular Mechanisms of Subcellular Localization of ABCGS and ABCG8
- ATP-Binding Cassette Proteins Involved in Glucose and Lipid Homeostasis
- Cholesterol and Plant Sterol Efflux from Cultured Intestinal Epithelial Cells Is Mediated by ATP-Binding Cassette Transporters