ABCC8 p.Leu183Pro
| Predicted by SNAP2: | A: N (82%), C: N (93%), D: N (53%), E: N (53%), F: N (93%), G: N (61%), H: N (87%), I: N (93%), K: D (53%), M: N (97%), N: N (57%), P: N (53%), Q: N (72%), R: N (66%), S: N (72%), T: N (93%), V: N (97%), W: N (61%), Y: N (57%), |
| Predicted by PROVEAN: | A: N, C: N, D: D, E: D, F: N, G: D, H: D, I: N, K: D, M: N, N: D, P: D, Q: D, R: D, S: N, T: N, V: N, W: D, Y: N, |
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[hide] Targeted degradation of ABC transporters in health... J Bioenerg Biomembr. 2007 Dec;39(5-6):489-97. Nikles D, Tampe R
Targeted degradation of ABC transporters in health and disease.
J Bioenerg Biomembr. 2007 Dec;39(5-6):489-97., [PMID:17972020]
Abstract [show]
ATP binding cassette (ABC) transporters comprise an extended protein family involved in the transport of a broad spectrum of solutes across membranes. They consist of a common architecture including two ATP-binding domains converting chemical energy into conformational changes and two transmembrane domains facilitating transport via alternating access. This review focuses on the biogenesis, and more precisely, on the degradation of mammalian ABC transporters in the endoplasmic reticulum (ER). We enlighten the ER-associated degradation pathway in the context of misfolded, misassembled or tightly regulated ABC transporters with a closer view on the cystic fibrosis transmembrane conductance regulator (CFTR) and the transporter associated with antigen processing (TAP), which plays an essential role in the adaptive immunity. Three rather different scenarios affecting the stability and degradation of ABC transporters are discussed: (1) misfolded domains caused by a lack of proper intra- and intermolecular contacts within the ABC transporters, (2) deficient assembly with auxiliary factors, and (3) arrest and accumulation of an intermediate or 'dead-end' state in the transport cycle, which is prone to be recognized by the ER-associated degradation machinery.
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92 Table 1 Degradation of ABC transporters ABC transporter Organism Initiation of degradation Ref. CFTR/ABCC7 (wt and ΔF508) Human Misfolding Jensen et al. (1995), Ward et al. (1995) SUR1/ABCC8 (wt and mutants) Human Lack of K(ATP) channel misfolding Crane and Aguilar-Bryan (2004); Yan et al. (2005) ABCG2 (C592G or C608G) Human Lack of intramolecular disulfide bond Wakabayashi et al. (2007) ALDP/ABCD1 (several mutants) Human Mutations in the NBD Takahashi et al. (2007) TAP2/ABCB3 Human Lack of TAP1 de la Salle et al. (1999), Heintke et al. (2003), Karttunen et al. (2001) TAP1/2/ABCB2/3 Human Lack of tapasin Garbi et al. (2003), Lehner et al. (1998), Papadopoulos and Momburg (2007) TAP1/2/ABCB2/3 Human Viral inhibitors UL49.5 and mK3 Boname et al. (2004), Koppers-Lalic et al. (2005), Lybarger et al. (2003), Wang et al. (2007) Pdr5 (ΔC-term and L183P) Yeast Misfolded NBD de Thozee et al. (2007) Yor1p (ΔF670) Yeast Space change in NBD Pagant et al. (2007) Instability and degradation of TAP2 in TAP1 deficiency (Bare Lymphocyte Syndrome, BLS) Molecules and disease-associated states that interfere with the stability of TAP are reconciled in this and the next chapter to reveal an overall understanding of TAP biogenesis.
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ABCC8 p.Leu183Pro 17972020:92:864
status: NEW