ABCA1 p.Lys171*
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[hide] Association of ABCA1 with syntaxin 13 and flotilli... Mol Biol Cell. 2004 Dec;15(12):5399-407. Epub 2004 Oct 6. Bared SM, Buechler C, Boettcher A, Dayoub R, Sigruener A, Grandl M, Rudolph C, Dada A, Schmitz G
Association of ABCA1 with syntaxin 13 and flotillin-1 and enhanced phagocytosis in tangier cells.
Mol Biol Cell. 2004 Dec;15(12):5399-407. Epub 2004 Oct 6., [PMID:15469992]
Abstract [show]
The ATP-binding cassette transporter A1 (ABCA1) facilitates the cellular release of cholesterol and choline-phospholipids to apolipoprotein A-I (apoA-I) and several studies indicate that vesicular transport is associated with ABCA1 function. Syntaxins play a major role in vesicular fusion and have also been demonstrated to interact with members of the ABC-transporter family. Therefore, we focused on the identification of syntaxins that directly interact with ABCA1. The expression of syntaxins and ABCA1 in cultured human monocytes during M-CSF differentiation and cholesterol loading was investigated and syntaxins 3, 6, and 13 were found induced in foam cells together with ABCA1. Immunoprecipitation experiments revealed a direct association of syntaxin 13 and full-length ABCA1, whereas syntaxin 3 and 6 failed to interact with ABCA1. The colocalization of ABCA1 and syntaxin 13 was also shown by immunofluorescence microscopy. Silencing of syntaxin 13 by small interfering RNA (siRNA) led to reduced ABCA1 protein levels and hence to a significant decrease in apoA-I-dependent choline-phospholipid efflux. ABCA1 is localized in Lubrol WX-insoluble raft microdomains in macrophages and syntaxin 13 and flotillin-1 were also detected in these detergent resistant microdomains along with ABCA1. Syntaxin 13, flotillin-1, and ABCA1 were identified as phagosomal proteins, indicating the involvement of the phagosomal compartment in ABCA1-mediated lipid efflux. In addition, the uptake of latex phagobeads by fibroblasts with mutated ABCA1 was enhanced when compared with control cells and the recombinant expression of functional ABCA1 normalized the phagocytosis rate in Tangier fibroblasts. It is concluded that ABCA1 forms a complex with syntaxin 13 and flotillin-1, residing at the plasma membrane and in phagosomes that are partially located in raft microdomains.
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50 Patient TD1 bears a homozygous K171X mutation, patients TD3 and TD5 display mutations that have been published previously (Bodzioch et al., 1999).
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ABCA1 p.Lys171* 15469992:50:31
status: NEW157 To further support the hypothesis that ABCA1 may regulate phagocytosis, the phagocytic activity of fibroblasts from control donors and fibroblasts isolated from the Tangier patients TD1 (yielding a mutation at K171X), TD3 II:4 and TD5 III:4 (Bodzioch et al., 1999) was measured by flow cytometry using fluorescent yellow green-labeled phagobeads.
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ABCA1 p.Lys171* 15469992:157:210
status: NEW49 Patient TD1 bears a homozygous K171X mutation, patients TD3 and TD5 display mutations that have been published previously (Bodzioch et al., 1999).
X
ABCA1 p.Lys171* 15469992:49:31
status: NEW159 To further support the hypothesis that ABCA1 may regulate phagocytosis, the phagocytic activity of fibroblasts from control donors and fibroblasts isolated from the Tangier patients TD1 (yielding a mutation at K171X), TD3 II:4 and TD5 III:4 (Bodzioch et al., 1999) was measured by flow cytometry using fluorescent yellow green-labeled phagobeads.
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ABCA1 p.Lys171* 15469992:159:210
status: NEW