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• W2912507780 abstract "The C. 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 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 adenosine triphosphatases (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." @default.
• W2912507780 created "2019-02-21" @default.
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• W2912507780 date "2019-01-01" @default.
• W2912507780 modified "2023-10-16" @default.
• W2912507780 title "Structure and function analysis of the <i>C. elegans</i> aminophospholipid translocase TAT–1" @default.
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• W2912507780 doi "https://doi.org/10.1242/jcs.227660" @default.
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