Isolation and characterization of novel mutations in CDC50, the non-catalytic subunit of the Drs2p phospholipid flippase

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Flippases (type 4 P-type ATPases) are believed to translocate phospholipids from the exoplasmic to the cytoplasmic leaflet in bilayer membranes. Since flippases are structurally similar to ion-transporting P-type ATPases such as the Ca2+ ATPase, one important question is how flippases have evolved to transport phospholipids instead of ions. We previously showed that a conserved membrane protein, Cdc50p, is required for the ER exit of the Drs2p flippase in yeast. However, Cdc50p is still associated with Drs2p after its transport to the endosomal/TGN membranes, and its function in the complex with Drs2p is unknown. In this study, we isolated novel temperature-sensitive (ts) cdc50 mutants whose products were still localized to endosomal/TGN compartments at the non-permissive temperature. Mutant Cdc50 proteins colocalized with Drs2p in endosomal/TGN compartments, and they co-immunoprecipitated with Drs2p. These cdc50-ts mutants exhibited defects in vesicle transport from early endosomes to the TGN as the cdc50 deletion mutant did. These results suggest that mutant Cdc50 proteins could be complexed with Drs2p, but the resulting Cdc50p-Drs2p complex is functionally defective at the non-permissive temperature. Cdc50p may play an important role for phospholipid translocation by Drs2p.

収録刊行物

  • The journal of biochemistry

    The journal of biochemistry 149(4), 423-432, 2011-04-01

    Japanese Biochemical Society

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各種コード

  • NII論文ID(NAID)
    10030584677
  • NII書誌ID(NCID)
    AA00694073
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    0021924X
  • NDL 記事登録ID
    11032116
  • NDL 雑誌分類
    ZR2(科学技術--生物学--生化学)
  • NDL 請求記号
    Z53-B472
  • データ提供元
    CJP書誌  NDL  IR 
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