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10.1371/journal.pone.0136779

http://scihub22266oqcxt.onion/10.1371/journal.pone.0136779
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suck abstract from ncbi


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pmid26406980
      PLoS+One 2015 ; 10 (9 ): e0136779
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  • The Role of Flexible Loops in Folding, Trafficking and Activity of Equilibrative Nucleoside Transporters #MMPMID26406980
  • Aseervatham J ; Tran L ; Machaca K ; Boudker O
  • PLoS One 2015[]; 10 (9 ): e0136779 PMID26406980 show ga
  • Equilibrative nucleoside transporters (ENTs) are integral membrane proteins, which reside in plasma membranes of all eukaryotic cells and mediate thermodynamically downhill transport of nucleosides. This process is essential for nucleoside recycling, and also plays a key role in terminating adenosine-mediated cellular signaling. Furthermore, ENTs mediate the uptake of many drugs, including anticancer and antiviral nucleoside analogues. The structure and mechanism, by which ENTs catalyze trans-membrane transport of their substrates, remain unknown. To identify the core of the transporter needed for stability, activity, and for its correct trafficking to the plasma membrane, we have expressed human ENT deletion mutants in Xenopus laevis oocytes and determined their localization, transport properties and susceptibility to inhibition. We found that the carboxyl terminal trans-membrane segments are essential for correct protein folding and trafficking. In contrast, the soluble extracellular and intracellular loops appear to be dispensable, and must be involved in the fine-tuning of transport regulation.
  • |*Amino Acid Sequence [MESH]
  • |*Protein Folding [MESH]
  • |*Sequence Deletion [MESH]
  • |Animals [MESH]
  • |Cell Membrane/genetics/*metabolism [MESH]
  • |Equilibrative Nucleoside Transporter 1/genetics/*metabolism [MESH]
  • |Humans [MESH]
  • |Protein Structure, Secondary [MESH]
  • |Protein Transport/physiology [MESH]


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