SLC3A24T2HC

Acts as a chaperone that facilitates biogenesis and trafficking of functional transporter heterodimers to the plasma membrane. Forms heterodimers with SLC7 family transporters (SLC7A5, SLC7A6, SLC7A7, SLC7A8, SLC7A10 and SLC7A11), a group of amino-acid antiporters. Heterodimers function as amino acid exchangers, the specificity of the substrate depending on the SLC7A subunit. Heterodimers SLC3A2/SLC7A6 or SLC3A2/SLC7A7 mediate the uptake of dibasic amino acids. Heterodimer SLC3A2/SLC7A11 functions as an antiporter by mediating the exchange of extracellular anionic L-cystine and intracellular L-glutamate across the cellular plasma membrane. SLC3A2/SLC7A10 translocates small neutral L- and D-amino acids across the plasma membrane (By similarity). SLC3A2/SLC75 or SLC3A2/SLC7A8 translocate neutral amino acids with broad specificity, thyroid hormones and L-DOPA. SLC3A2 is essential for the plasma membrane localization, stability, and transport activity of SLC7A5 and SLC7A8. When associated with LAPTM4B, the SLC3A2/SLC7A5 heterodimer is recruited to lysosomes to promote leucine uptake into these organelles, and thereby mediates mTORC1 activation. Modulates integrin-related signaling and is essential for integrin-dependent cell spreading, migration and tumor progression

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(Microbial infection) In case of hepatitis C virus/HCV infection, the complex formed by SLC3A2 and SLC7A5/LAT1 plays a role in HCV propagation by facilitating viral entry into host cell and increasing L-leucine uptake-mediated mTORC1 signaling activation, thereby contributing to HCV-mediated pathogenesis

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(Microbial infection) Acts as a receptor for malaria parasite Plasmodium vivax (Thai isolate) in immature red blood cells

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Disulfide-linked heterodimer with a non-glycosylated catalytic light subunit (SLC7A5, SLC7A6, SLC7A7, SLC7A8, SLC7A10 or SLC7A11). Interacts with TLCD3A/CT120. Interacts with ICAM1. Constitutively and specifically associates with beta-1 integrins (alpha-2/beta-1, alpha-3/beta-1, alpha-5/beta-1 and alpha-6/beta-1), but minimally with alpha-4/beta-1. Interacts with LAPTM4B; recruits SLC3A2 and SLC7A5/LAT1 to lysosomes to promote leucine uptake into these organelles and is required for mTORC1 activation

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(Microbial infection) Interacts with hepatitis C virus/HCV envelope glycoprotein E2; the interaction may facilitate viral entry into host cell

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Apical cell membrane; Cell membrane / Single-pass type II membrane protein; Cell junction; Lysosome membrane; Melanosome; Basolateral cell membrane; Localized at the plasma membrane when associated with SLC7A5/LAT1 or SLC7A8/LAT2. Localized to the apical membrane of placental syncytiotrophoblastic cells. Recruited to lysosomes by LAPTM4B. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Located selectively at cell-cell adhesion sites (By similarity). Colocalized with SLC7A8/LAT2 at the basolateral membrane of kidney proximal tubules and small intestine epithelia. Expressed in both luminal and abluminal membranes of brain capillary endothelial cells (By similarity)

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Expression is induced in resting peripheral blood T-lymphocytes following PHA stimulation. Expression increases at the time of maximal DNA synthesis, in fibroblasts stimulated to divide. Expression and the uptake of leucine is stimulated in mononuclear, cytotrophoblast-like choriocarcinoma cells by combined treatment with PMA and calcium ionophore. Up-regulated in response to hydrogen peroxide. Highly expressed in various cancer types

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(Microbial infection) Up-regulated upon hepatitis C virus/HCV infection via NS3-A4 viral protein complex; the up-regulation is mediated by oxidative stress. Up-regulation of the complex formed by SLC3A2 and SLC7A5/LAT1 upon hepatitis C virus/HCV infection

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