SLC44A1 Membrane Protein Introduction

Introduction of SLC44A1

Solute carrier family 44 member 1 (SLC44A1), also known as CDw92 or CTL1, is a transmembrane protein that in human is encoded by SLC44A1 gene. SLC44A1 belongs to the choline transporter-like (CTL) family and is identified as a Naþ-independent, intermediate-affinity transporter of choline. SLC44A1 is broadly expressed in various cells of the hematopoietic system. It is also found in the human central nervous system (CNS), including neuronal, glial and endothelial cells.

Function of SLC44A1 Membrane Protein

SLC44A1 has been considered as a key mediator of choline transport across both the plasma membrane and the mitochondrial membrane, and it might mediate choline transport into and out of mitochondria to ensure an immediate sink of cellular choline generated from PC and sphingomyelin metabolism. SLC44A1 may also play a role in membrane synthesis and myelin production. The SLC44A1 choline transport system utilizes a directed H⁺ gradient as a driving force, and its transport function is in cooperation with Naþ/Hþ exchangers. In addition, it has been indicated that malfunction of SLC44A1 could have significant implications in nervous system development and repair following injury, as well as in neurodegenerative diseases. A study focused on the small cell lung carcinoma shows that the functional inhibition of SLC44A1 could promote apoptotic cell death. And thus, the SLC44A1-mediated choline transport system provides a potential novel target for therapeutic intervention. Furthermore, SLC44A1 may also play a role in the transport of various cationic drugs as a drug transporter in the blood-brain barrier (BBB).

Fig.1 Choline transporter CTL1 locates at the trans-Golgi network (TGN), a post-Golgi compartment acting as a central hub in the cell where endosomal plasma membrane recycling takes place as well as secretory sorting to plasma membrane and trafficking to late endosomes. (Boutté, 2018)

Application of SLC44A1 Membrane Protein in Literature

1. Nagashima F., et al. Molecular and functional characterization of choline transporter-like proteins in esophageal cancer cells and potential therapeutic targets. Biomol Ther (Seoul). 2018, 26(4):399-408. PubMed ID: 29223141
   
   

   The results of this study show that extracellular choline is mainly transported via CTL1 and the functional inhibition of CTL1 by cationic drugs could promote apoptotic cell death.

2. Heffernan C., et al. Nectin-like 4 complexes with choline transporter-like protein-1 and regulates Schwann cell choline homeostasis and lipid biogenesis in vitro. J Biol Chem. 2017, 292(11):4484-4498. PubMed ID: 28119456
   
   

   This study identifies CTL1 as a putative complexing partner with NECL4, by mass spectrometry and western blotting techniques.

3. Wang Y., et al. Arabidopsis choline transporter-like 1 (CTL1) regulates secretory trafficking of auxin transporters to control seedling growth. PLoS Biol. 2017, 15(12):e2004310. PubMed ID: 29283991
   
   

   Authors of this study reveal that the phospholipids, sphingolipids, and other membrane lipids are significantly altered in the ctl1 mutant, which links the CTL1 function to lipid homeostasis.

4. Gao Y.Q., et al. A new vesicle trafficking regulator CTL1 plays a crucial role in ion homeostasis. PLoS Biol. 2017, 15(12):e2002978. PubMed ID: 29284002
   
   

   Authors of this article demonstrate that CTL1 plays a role in regulating vesicle trafficking and therefore is required for the trafficking of proteins essential for ion transport and PD development.

5. Iwao B., et al. Functional expression of choline transporter like-protein 1 (CTL1) and CTL2 in human brain microvascular endothelial cells. Neurochem Int. 2016, 93:40-50. PubMed ID: 26746385
   
   

   Authors of this article investigate the molecular and functional characterization of choline transporter in human brain microvascular endothelial cells (hBMECs), and they suggest that choline is predominantly transported by an intermediate-affinity choline transport system, CTL1 and CTL2, in hBMECs.

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Reference

1. Boutté Y. (2018). Lipids at the crossroad: Shaping biological membranes heterogeneity defines trafficking pathways. PLoS biology. 16(2), e2005188.

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