scholarly journals Amino acid transporter SLC6A14 depends on heat shock protein HSP90 in trafficking to the cell surface

2019 ◽  
Vol 1866 (10) ◽  
pp. 1544-1555 ◽  
Author(s):  
Karolina Rogala-Koziarska ◽  
Łukasz Samluk ◽  
Katarzyna A. Nałęcz
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Cell Surface ◽  
Heat Shock Protein ◽  
Amino Acid Transporter ◽  
Acid Transporter

Galectin-lattice sustains function of cationic amino acid transporter and insulin secretion of pancreatic β cells

2020 ◽  
Vol 167 (6) ◽  
pp. 587-596 ◽  
Author(s):  
Kento Maeda ◽  
Masayoshi Tasaki ◽  
Yukio Ando ◽  
Kazuaki Ohtsubo
Keyword(s):  
Insulin Secretion ◽  
Amino Acid ◽  
Cell Surface ◽  
Amino Acid Transporter ◽  
Cell Surface Expression ◽  
Cationic Amino Acid Transporter ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
Cationic Amino Acid ◽  
Acid Transporter

Abstract Maintenance of cell surface residency and function of glycoproteins by lectins are essential for regulating cellular functions. Galectins are β-galactoside-binding lectins and form a galectin-lattice, which regulates stability, clustering, membrane sub-domain localization and endocytosis of plasmalemmal glycoproteins. We have previously reported that galectin-2 (Gal-2) forms a complex with cationic amino acid transporter 3 (CAT3) in pancreatic β cells, although the biological significance of the molecular interaction between Gal-2 and CAT3 has not been elucidated. In this study, we demonstrated that the structure of N-glycan of CAT3 was either tetra- or tri-antennary branch structure carrying β-galactosides, which works as galectin-ligands. Indeed, CAT3 bound to Gal-2 using β-galactoside epitope. Moreover, the disruption of the glycan-mediated bindings between galectins and CAT3 significantly reduced cell surface expression levels of CAT3. The reduced cell surface residency of CAT3 attenuated the cellular arginine uptake activities and subsequently reduced nitric oxide production, and thus impaired the arginine-stimulated insulin secretion of pancreatic β cells. These results indicate that galectin-lattice stabilizes CAT3 by preventing endocytosis to sustain the arginine-stimulated insulin secretion of pancreatic β cells. This provides a novel cell biological insight into the endocrinological mechanism of nutrition metabolism and homeostasis.

Cell-surface receptor for ecotropic murine retroviruses is a basic amino-acid transporter

Nature ◽  
1991 ◽  
Vol 352 (6337) ◽  
pp. 729-731 ◽  
Author(s):  
Hao Wang ◽  
Michael P. Kavanaugh ◽  
R. Alan North ◽  
David Kabat
Keyword(s):  
Amino Acid ◽  
Cell Surface ◽  
Basic Amino Acid ◽  
Amino Acid Transporter ◽  
Cell Surface Receptor ◽  
Surface Receptor ◽  
Acid Transporter

scholarly journals Modulation of ecotropic murine retroviruses by N-linked glycosylation of the cell surface receptor/amino acid transporter.

1996 ◽  
Vol 70 (10) ◽  
pp. 6884-6891 ◽  
Author(s):  
H Wang ◽  
E Klamo ◽  
S E Kuhmann ◽  
S L Kozak ◽  
M P Kavanaugh ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cell Surface ◽  
Amino Acid Transporter ◽  
Cell Surface Receptor ◽  
Surface Receptor ◽  
Acid Transporter

scholarly journals ASC-1, PAT2, and P2RX5 are cell surface markers for white, beige, and brown adipocytes

2014 ◽  
Vol 6 (247) ◽  
pp. 247ra103-247ra103 ◽  
Author(s):  
Siegfried Ussar ◽  
Kevin Y. Lee ◽  
Simon N. Dankel ◽  
Jeremie Boucher ◽  
Max-Felix Haering ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cell Surface ◽  
Cell Types ◽  
Amino Acid Transporter ◽  
Specific Cell ◽  
Surface Markers ◽  
Cell Surface Markers ◽  
Brown Adipocytes ◽  
Beige Adipocytes ◽  
Acid Transporter

White, beige, and brown adipocytes are developmentally and functionally distinct but often occur mixed together within individual depots. To target white, beige, and brown adipocytes for diagnostic or therapeutic purposes, a better understanding of the cell surface properties of these cell types is essential. Using a combination of in silico, in vitro, and in vivo methods, we have identified three new cell surface markers of adipose cell types. The amino acid transporter ASC-1 is a white adipocyte–specific cell surface protein, with little or no expression in brown adipocytes, whereas the amino acid transporter PAT2 and the purinergic receptor P2RX5 are cell surface markers expressed in classical brown and beige adipocytes in mice. These markers also selectively mark brown/beige and white adipocytes in human tissue. Thus, ASC-1, PAT2, and P2RX5 are membrane surface proteins that may serve as tools to identify and target white and brown/beige adipocytes for therapeutic purposes.

scholarly journals Trafficking to the Cell Surface of Amino Acid Transporter SLC6A14 Upregulated in Cancer Is Controlled by Phosphorylation of SEC24C Protein by AKT Kinase

Cells ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1800
Author(s):  
Vasylyna Kovalchuk ◽  
Katarzyna A. Nałęcz
Keyword(s):  
Plasma Membrane ◽  
Amino Acid ◽  
Cell Surface ◽  
Cancer Cell ◽  
Cancer Cell Line ◽  
Amino Acid Transporter ◽  
Proximity Ligation Assay ◽  
Cancer Cell Survival ◽  
Acid Transporter ◽  
Er Export

Cancer cells need a constant supply of nutrients. SLC6A14, an amino acid transporter B0,+ (ATB0,+) that is upregulated in many cancers, transports all but acidic amino acids. In its exit from the endoplasmic reticulum (ER), it is recognized by the SEC24C subunit of coatomer II (COPII) for further vesicular trafficking to the plasma membrane. SEC24C has previously been shown to be phosphorylated by protein kinase B/AKT, which is hyper-activated in cancer; therefore, we analyzed the influence of AKT on SLC6A14 trafficking to the cell surface. Studies on overexpressed and endogenous transporters in the breast cancer cell line MCF-7 showed that AKT inhibition with MK-2206 correlated with a transient increase of the transporter in the plasma membrane, not resulting from the inhibition of ER-associated protein degradation. Two-dimensional electrophoresis demonstrated the decreased phosphorylation of SLC6A14 and SEC24C upon AKT inhibition. A proximity ligation assay confirmed this conclusion: AKT inhibition is correlated with decreased SLC6A14 phosphothreonine and SEC24C phosphoserine. Augmented levels of SLC6A14 in plasma membrane led to increased leucine transport. These results show that the inactivation of AKT can rescue amino acid delivery through SLC6A14 trafficking to the cell surface, supporting cancer cell survival. The regulation of the ER export of the amino acid transporter seems to be a novel function of AKT.

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