Position 834 in TM6 plays an important role in cholesterol and phosphatidylcholine transport by ABCA1

We showed that L834 is critical for the function of ATP-binding cassette protein A1

Shimpei Itoh; Kohjiro Nagao; Yasuhisa Kimura; Michinori Matsuo; Noriyuki Kioka; Kazumitsu Ueda

2015

Scholarcy highlights

  • To identify the amino acid residues of ATP-binding cassette protein A1 involved in substrate recognition and transport, we applied arginine scan mutagenesis to residues L821–E843 of human ABCA1 and predicted the environment to which each residue is exposed
  • The relative surface expression of each mutant suggested that residues L821–E843 pass through the plasma membrane as TM6, and the four residues of TM6 are exposed to the hydrophilic internal cavity of ABCA1
  • We showed that L834 is critical for the function of ABCA1
  • We showed that L834 is critical for the function of ATP-binding cassette protein A1

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