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Structure and function analysis of the C. elegans aminophospholipid translocase TAT-1.

Chen, Yu-Zen; Klöditz, Katharina; Lee, Eui-Seung; Nguyen, Diemmy Pham; Yuan, Quan; Johnson, Jack; Lee-Yow, Yannick; Hall, Adam; Mitani, Shohei; Xia, Ning-Shao; Fadeel, Bengt; Xue, Ding.
J Cell Sci; 132(5)2019 Feb 28.
Artigo em Inglês | MEDLINE | ID: mdl-30683797
The Caenorhabditis elegans aminophospholipid translocase TAT-1 maintains phosphatidylserine (PS) asymmetry in the plasma membrane and regulates endocytic transport. Despite these important functions, the structure-function relationship of this protein is poorly understood. Taking advantage of the tat-1 mutations identified by the C. elegans million mutation project, we investigated the effects of 16 single amino acid substitutions on the two functions of the TAT-1 protein. Two substitutions that alter a highly conserved PISL motif in the fourth transmembrane domain and a highly conserved DKTGT phosphorylation motif, respectively, disrupt both functions of TAT-1, leading to a vesicular gut defect and ectopic PS exposure on the cell surface, whereas most other substitutions across the TAT-1 protein, often predicted to be deleterious by bioinformatics programs, do not affect the functions of TAT-1. These results provide in vivo evidence for the importance of the PISL and DKTGT motifs in P4-type ATPases and improve our understanding of the structure-function relationship of TAT-1. Our study also provides an example of how the C. elegans million mutation project helps decipher the structure, functions, and mechanisms of action of important genes.
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