@article{302e8ccbfcbf4684b4c539656abafe74,
title = "Protean permeases: Diverse roles for membrane transport proteins in kinetoplastid protozoa",
abstract = "Kinetoplastid parasites such as Trypanosoma brucei, Trypanosoma cruzi, and Leishmania species rely upon their insect and vertebrate hosts to provide a plethora of nutrients throughout their life cycles. Nutrients and ions critical for parasite survival are taken up across the parasite plasma membrane by transporters and channels, polytopic membrane proteins that provide substrate-specific pores across the hydrophobic barrier. However, transporters and channels serve a wide range of biological functions beyond uptake of nutrients. This article highlights the diversity of activities that these integral membrane proteins serve and underscores the emerging complexity of their functions.",
keywords = "Channels, Drug sensitivity, Kinetoplastid parasites, Organelles, Sensing, Transporters",
author = "Landfear, {Scott M.}",
note = "Funding Information: Research in the SML laboratory was funded by National Institutes of Health grants AI121160 , AI1144822 , and AI114842 . I thank Phil Yates and Felice Kelly for thoughtful comments on the manuscript and Laramie Studio, Portland, OR, USA for preparing the figure. A recently published article (F. Rojas et al., Oligopeptide signaling through TbGPR89 drives trypanosome quorum sensing, Cell 176, 2019, 1-12) demonstrates that a novel oligopeptide transporter, TbGPR89, plays a critical role in quorum sensing that allows the developmental transition of long slender (LS) bloodstream form African trypanosomes into short stumpy forms (SF) that are adapted for differentiation into procyclic forms once taken up by the tsetse fly. This permease mediates uptake into the cytosol of LS forms of extracellular oligopeptides, which function as cell density-dependent Stumpy Inducing Factor (SIF), and thus allows the LS to SF transformation to occur in response to SIF. Funding Information: Research in the SML laboratory was funded by National Institutes of Health grants AI121160, AI1144822, and AI114842. I thank Phil Yates and Felice Kelly for thoughtful comments on the manuscript and Laramie Studio, Portland, OR, USA for preparing the figure. A recently published article (F. Rojas et al., Oligopeptide signaling through TbGPR89 drives trypanosome quorum sensing, Cell 176, 2019, 1-12) demonstrates that a novel oligopeptide transporter, TbGPR89, plays a critical role in quorum sensing that allows the developmental transition of long slender (LS) bloodstream form African trypanosomes into short stumpy forms (SF) that are adapted for differentiation into procyclic forms once taken up by the tsetse fly. This permease mediates uptake into the cytosol of LS forms of extracellular oligopeptides, which function as cell density-dependent Stumpy Inducing Factor (SIF), and thus allows the LS to SF transformation to occur in response to SIF. Publisher Copyright: {\textcopyright} 2018 Elsevier B.V.",
year = "2019",
month = jan,
doi = "10.1016/j.molbiopara.2018.12.006",
language = "English (US)",
volume = "227",
pages = "39--46",
journal = "Molecular and Biochemical Parasitology",
issn = "0166-6851",
publisher = "Elsevier",
}