Posttranslational negative regulation of glycosylated and non-glycosylated BCRP expression by Derlin-1

Biochemical and Biophysical Research Communications

Volumn 404, Issue 3, 2011, Pages 853-858

  Sugiyama, Takashi ^a   Shuto, Tsuyoshi ^a   Suzuki, Shingo ^a   Sato, Takashi ^a   Koga, Tomoaki ^a   Suico, Mary Ann ^a   Kusuhara, Hiroyuki ^b   Sugiyama, Yuichi ^b   Cyr, Douglas M ^c   Kai, Hirofumi ^a  

^a KUMAMOTO UNIVERSITY   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

BCRP; Derlin 1; ER associated degradation (ERAD); N linked glycosylation; Posttranslational regulation

Indexed keywords

BREAST CANCER RESISTANCE PROTEIN; DERLIN 1 PROTEIN; MEMBRANE PROTEIN; TUNICAMYCIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

ARTICLE; CELL MEMBRANE; CELL MIGRATION; CELLULAR DISTRIBUTION; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; GLYCOSYLATION; GOLGI COMPLEX; HUMAN; HUMAN CELL; MEMBRANE TRANSPORT; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN PROCESSING; PROTEIN STABILITY; REGULATORY MECHANISM; WILD TYPE; YEAST;

ATP-BINDING CASSETTE TRANSPORTERS; ENDOPLASMIC RETICULUM; GLYCOSYLATION; HUMANS; MEMBRANE PROTEINS; NEOPLASM PROTEINS; PROTEIN PROCESSING, POST-TRANSLATIONAL;

EID: 78751610987     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.12.074     Document Type: Article

References (28)

1. Oldham M.L., Davidson A.L., Chen J. Structural insights into ABC transporter mechanism. Curr. Opin. Struct. Biol. 2008, 18:726-733.
2. Ni Z., Bikadi Z., Rosenberg M.F., et al. Structure and function of the human breast cancer resistance protein (BCRP/ABCG2). Curr. Drug Metab. 2010, 11:603-617.
3. Kusuhara H., Sugiyama Y. ATP-binding cassette, subfamily G (ABCG family). Pflugers Arch. Eur. J. Physiol. 2007, 453:735-744.
4. Vlaming M.L., Lagas J.S., Schinkel A.H. Physiological and pharmacological roles of ABCG2 (BCRP): recent findings in Abcg2 knockout mice. Adv. Drug Deliv. Rev. 2009, 61:14-25.
5. Matsuo H., Takada T., Ichida K., et al. Common defects of ABCG2, a high-capacity urate exporter, cause gout: a function-based genetic analysis in a Japanese population. Sci. Transl. Med. 2009, 1:5ra11.
6. Noguchi K., Katayama K., Mitsuhashi J., et al. Functions of the breast cancer resistance protein (BCRP/ABCG2) in chemotherapy. Adv. Drug Deliv. Rev. 2009, 61:26-33.
7. Yoh K., Ishii G., Yokose T., et al. Breast cancer resistance protein impacts clinical outcome in platinum-based chemotherapy for advanced non-small cell lung cancer. Clin. Cancer Res. 2004, 10:1691-1697.
8. Wakabayashi-Nakao K., Tamura A., Furukawa T., et al. Quality control of human ABCG2 protein in the endoplasmic reticulum: ubiquitination and proteasomal degradation. Adv. Drug Deliv. Rev. 2009, 61:66-72.
9. Nakagawa H., Wakabayashi-Nakao K., Tamura A., et al. Disruption of N-linked glycosylation enhances ubiquitin-mediated proteasomal degradation of the human ATP-binding cassette transporter ABCG2. FEBS J. 2009, 276:7237-7252.
10. Furukawa T., Wakabayashi K., Tamura A., et al. Major SNP (Q141K) variant of human ABC transporter ABCG2 undergoes lysosomal and proteasomal degradations. Pharm. Res. 2009, 26:469-479.
11. Nakagawa H., Tamura A., Wakabayashi K., et al. Ubiquitin-mediated proteasomal degradation of non-synonymous SNP variants of human ABC transporter ABCG2. Biochem. J. 2008, 411:623-631.
12. Knop M., Finger A., Braun T., et al. Der1 A novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J. 1996, 15:753-763.
13. Shimasaki S., Koga T., Shuto T., et al. Endoplasmic reticulum stress increases the expression and function of toll-like receptor-2 in epithelial cells. Biochem. Biophys. Res. Commun. 2010, 402:235-240.
14. Taura M., Eguma A., Suico M.A., et al. P53 regulates Toll-like receptor 3 expression and function in human epithelial cell lines. Mol. Cell. Biol. 2008, 28:6557-6567.
15. Sugahara T., Koga T., Ueno-Shuto K., et al. Calreticulin positively regulates the expression and function of epithelial sodium channel. Exp. Cell. Res. 2009, 315:3294-3300.
16. Harada K., Okiyoneda T., Hashimoto Y., et al. Calreticulin negatively regulates the cell surface expression of cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 2006, 281:12841-12848.
17. Ballar P., Ors A.U., Yang H., et al. Differential regulation of CFTRDeltaF508 degradation by ubiquitin ligases gp78 and Hrd1. Int. J. Biochem. Cell Biol. 2009, 42:167-173.
18. Younger J.M., Chen L., Ren H.Y., et al. Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator. Cell 2006, 126:571-582.
19. Wang L., Dong H., Soroka C.J., et al. Degradation of the bile salt export pump at endoplasmic reticulum in progressive familial intrahepatic cholestasis type II. Hepatology 2008, 48:1558-1569.
20. Klausner R.D., Donaldson J.G., Lippincott-Schwartz J. Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 1992, 116:1071-1080.
21. Lee D.H., Goldberg A.L. Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae. J. Biol. Chem. 1996, 271:27280-27284.
22. Nikles D., Tampe R. Targeted degradation of ABC transporters in health and disease. J. Bioenerg. Biomembr. 2007, 39:489-497.
23. Amaral M.D. CFTR and chaperones: processing and degradation. J. Mol. Neurosci. 2004, 23:41-48.
24. Turnbull E.L., Rosser M.F., Cyr D.M. The role of the UPS in cystic fibrosis. BMC Biochem. 2007, 8(Suppl 1):S11.
25. Sun F., Zhang R., Gong X., et al. Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants. J. Biol. Chem. 2006, 281:36856-36863.
26. Bernardi K.M., Williams J.M., Kikkert M., et al. The E3 ubiquitin ligases Hrd1 and gp78 bind to and promote cholera toxin retro-translocation. Mol. Biol. Cell 2010, 21:140-151.
27. Polgar O., Ediriwickrema L.S., Robey R.W., et al. Arginine 383 is a crucial residue in ABCG2 biogenesis. Biochim. Biophys. Acta. Biomembr. 2009, 1788:1434-1443.
28. Polgar O., Ozvegy-Laczka C., Robey R.W., et al. Mutational studies of G553 in TM5 of ABCG2: a residue potentially involved in dimerization. Biochemistry 2006, 45:5251-5260.