caa a22 4500 463208315 CHVBK 20180405153132.0 cr unu---uuuuu 170326e20071201xx s 000 0 eng 10.1007/s10863-007-9120-z doi (NATIONALLICENCE)springer-10.1007/s10863-007-9120-z Targeted degradation of ABC transporters in health and disease [Elektronische Daten] [Daphne Nikles, Robert Tampé] 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. Springer Science+Business Media, LLC, 2007 ABC transporter nationallicence ER-associated degradation nationallicence Membrane protein nationallicence Misassembly nationallicence Misfolding nationallicence Ubiquitin proteasome pathway nationallicence Nikles Daphne Institute of Biochemistry, Biocenter, Johann Wolfgang Goethe-University, Max-von-Laue-Str. 9, 60348, Frankfurt am Main, Germany aut Tampé Robert Institute of Biochemistry, Biocenter, Johann Wolfgang Goethe-University, Max-von-Laue-Str. 9, 60348, Frankfurt am Main, Germany aut Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 489-497 0145-479X 39:5-6<489 2007 39 10863 https://doi.org/10.1007/s10863-007-9120-z text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10863-007-9120-z text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Nikles Daphne Institute of Biochemistry, Biocenter, Johann Wolfgang Goethe-University, Max-von-Laue-Str. 9, 60348, Frankfurt am Main, Germany aut NATIONALLICENCE 700 1- Tampé Robert Institute of Biochemistry, Biocenter, Johann Wolfgang Goethe-University, Max-von-Laue-Str. 9, 60348, Frankfurt am Main, Germany aut NATIONALLICENCE 773 0- Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 489-497 0145-479X 39:5-6<489 2007 39 10863 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer