ABCB9 p.Leu137Ala
| Predicted by SNAP2: | A: D (75%), C: D (80%), D: D (95%), E: D (95%), F: D (80%), G: D (95%), H: D (91%), I: D (71%), K: D (95%), M: D (59%), N: D (95%), P: D (95%), Q: D (91%), R: D (95%), S: D (91%), T: D (91%), V: D (63%), W: D (91%), Y: D (80%), |
| Predicted by PROVEAN: | A: D, C: D, 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: D, T: N, V: N, W: N, Y: N, |
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[hide] Tuning the cellular trafficking of the lysosomal p... Traffic. 2010 Mar;11(3):383-93. Demirel O, Bangert I, Tampe R, Abele R
Tuning the cellular trafficking of the lysosomal peptide transporter TAPL by its N-terminal domain.
Traffic. 2010 Mar;11(3):383-93., [PMID:20377823]
Abstract [show]
The homodimeric ATP-binding cassette (ABC) transport complex TAPL (transporter associated with antigen processing-like, ABCB9) translocates a broad spectrum of peptides from the cytosol into the lumen of lysosomes. The presence of an extra N-terminal transmembrane domain (TMD0) lacking any sequence homology to known proteins distinguishes TAPL from most other ABC transporters of its subfamily. By dissecting TAPL, we could assign distinct functions to the core complex and TMD0. The core-TAPL complex, composed of six predicted transmembrane helices and a nucleotide-binding domain, is sufficient for peptide transport, showing that the core transport complex is correctly targeted to and assembled in the membrane. Strikingly, in contrast to the full-length transporter, the core translocation complex is targeted preferentially to the plasma membrane. However, TMD0 alone, comprising a putative four transmembrane helix bundle, traffics to lysosomes. Upon coexpression, TMD0 forms a stable non-covalently linked complex with the core translocation machinery and guides core-TAPL into lysosomal compartments. Therefore, TMD0 represents a unique domain, which folds independently and encodes the information for lysosomal targeting. These outcomes are discussed in respect of trafficking, folding and function of TAPL.
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No. Sentence Comment
84 For immunofluorescence microscopy, HeLa cells, transiently transfected with wt-TAPL, core-TAPL, TMD0 or TAPL-L136A/L137A, were fixed and stained with anti-TAPL or anti-myc antibody.
X
ABCB9 p.Leu137Ala 20377823:84:115
status: NEW89 Expressed in HeLa cells, the L136A/L137A mutant was also localized in the lysosomal compartment (Pearson coefficient of 0.5), thereby ruling out the possibility that this dileucine motif is the exclusive lysosomal targeting signal of TAPL.
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ABCB9 p.Leu137Ala 20377823:89:35
status: NEW