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Titolo:
ATP-binding cassette transporter A1 contains an NH2-terminal signal anchorsequence that translocates the protein's first hydrophilic domain to the exoplasmic space
Autore:
Fitzgerald, ML; Mendez, AJ; Moore, KJ; Andersson, LP; Panjeton, HA; Freeman, MW;
Indirizzi:
Massachusetts Gen Hosp, Lipid Metab Unit, Boston, MA 02114 USA Massachusetts Gen Hosp Boston MA USA 02114 tab Unit, Boston, MA 02114 USA Harvard Univ, Sch Med, Boston, MA 02114 USA Harvard Univ Boston MA USA 02114 vard Univ, Sch Med, Boston, MA 02114 USA Univ Miami, Sch Med, Diabet Res Inst, Miami, FL 33101 USA Univ Miami Miami FL USA 33101 h Med, Diabet Res Inst, Miami, FL 33101 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 18, volume: 276, anno: 2001,
pagine: 15137 - 15145
SICI:
0021-9258(20010504)276:18<15137:ACTACA>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
TANGIER-DISEASE; CHOLESTEROL EFFLUX; MONOCLONAL-ANTIBODIES; CELLULAR CHOLESTEROL; HDL CHOLESTEROL; ABCA1 GENE; MUTATIONS; RECEPTOR; PROMOTER; CLONING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Freeman, MW Massachusetts Gen Hosp, Lipid Metab Unit, Boston, MA 02114 USAMassachusetts Gen Hosp Boston MA USA 02114 ston, MA 02114 USA
Citazione:
M.L. Fitzgerald et al., "ATP-binding cassette transporter A1 contains an NH2-terminal signal anchorsequence that translocates the protein's first hydrophilic domain to the exoplasmic space", J BIOL CHEM, 276(18), 2001, pp. 15137-15145

Abstract

Mutations in the ATP-binding cassette transporter A1 (ABCA1) transporter are associated with Tangier disease and a defect in cellular cholesterol efflux, The amino terminus of the ABCA1 transporter has two putative in-frame translation initiation sites, 60 amino acids apart. A cluster of hydrophobic amino acids form a potentially cleavable signal sequence in this 60-residue extension. We investigated the functional role of this extension and found that it was required for stable protein expression of transporter constructs containing any downstream transmembrane domains. The extension directed transporter translocation across the ER membrane with an orientation thatresulted in glycosylation of amino acids immediately distal to the signal sequence. Neither the native signal sequence nor a green fluorescent protein tag, fused at the amino terminus, was cleaved from ABCA1. The green fluorescent protein fusion protein had efflux activity comparable with wild typeABCA1 and demonstrated a predominantly plasma membrane distribution in transfected cells. These data establish a requirement for the upstream 60 amino acids of ABCA1. This region contains an uncleaved signal anchor sequence that positions the amino terminus in a type II orientation leading to the extracellular presentation of an similar to 600-amino acid loop in which loss-of-function mutations cluster in Tangier disease patients.

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Documento generato il 06/06/20 alle ore 08:06:14