ABCMdb

ABCB10 p.Leu46Gln

None has been submitted yet.

Publications

PMID: 15215243 [PubMed] Graf SA et al: "Targeting, import, and dimerization of a mammalian mitochondrial ATP binding cassette (ABC) transporter, ABCB10 (ABC-me)."

No. Sentence Comment

9 Disruption of its hydrophobic character by the mutation L46Q/ I47Q, however, greatly diminishes its efficacy. Login to comment
229 We removed one hydrophobic residue pair with the double mutation L46Q/I47Q. Login to comment
243 Mutation MMCC n Wild type 0.77 Ϯ 0.02 12 aa 36-70-R41A 0.71 Ϯ 0.04 12 aa 36-70-R55A 0.76 Ϯ 0.03 12 aa 36-70-R41A-R55A 0.74 Ϯ 0.03 28 aa 36-70-R41P 0.73 Ϯ 0.02 19 aa 36-70-A42P 0.75 Ϯ 0.03 16 ing-The flanking thirds of the mTP, aa 1-35 and 71-105, only partially rescue the effect of the L46Q/I47Q mutations on aa 36-70, demonstrating that the Leu46 -Ile47 hydrophobic pair of the mTP of ABCB10 is essential for its mitochondrial targeting (Fig. 4C). Login to comment
246 The R41A/L46Q/I47Q mutations were carried out in full-length ABCB10 (715 aa) fused to EGFP (Fig. 4E). Login to comment
257 B, the L46Q/I47Q mutant is additionally susceptible to reduction of targeting efficiency by R41A mutation. Login to comment
258 The asterisk indicates significant difference from aa 36-70-L46Q/I47Q. Login to comment
259 C and D, rejoining aa 1-35 and 71-105 to aa 36-70-L46Q/I47Q and aa 36-70-L46Q/I47Q/R41A partially restores mitochondrial targeting. Login to comment
262 E, fusing aa 106-715 to aa 1-105-L46Q/I47Q/R41A restores mitochondrial targeting to that of wild-type ABCB10. Login to comment
316 On the contrary, the hydrophobic residues responsible for Tom20 interaction must meet stringent accessibility and location requirements, since all nine additional hydrophobic pentapeptide motifs of the aforementioned type introduced by the flanking regions failed to completely rescue the L46Q/I47Q mutation. Login to comment