scholarly journals A guide to plasma membrane solute carrier proteins

FEBS Journal ◽  
2020 ◽  
Author(s):  
Mattia D. Pizzagalli ◽  
Ariel Bensimon ◽  
Giulio Superti‐Furga
Keyword(s):  
Plasma Membrane ◽  
Carrier Proteins ◽  
Solute Carrier

scholarly journals Sequence and Chromosomal Assignment of a Novel cDNA Identified by Immunoscreening of a Thyroid Expression Library: Similarity to a Family of Mitochondrial Solute Carrier Proteins

1989 ◽  
Vol 3 (9) ◽  
pp. 1498-1508 ◽  
Author(s):  
Raffaele Zarrilli ◽  
Edward L. Oates ◽  
O. Wesley McBride ◽  
Michael I. Lerman ◽  
John Y. Chan ◽  
...  
Keyword(s):  
Chromosomal Assignment ◽  
Carrier Proteins ◽  
Expression Library ◽  
Solute Carrier

The Candida albicans plasma membrane protein Rch1p, a member of the vertebrate SLC10 carrier family, is a novel regulator of cytosolic Ca2+ homoeostasis

2012 ◽  
Vol 444 (3) ◽  
pp. 497-502 ◽  
Author(s):  
Linghuo Jiang ◽  
Joerg Alber ◽  
Jihong Wang ◽  
Wei Du ◽  
Xuexue Yang ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Candida Albicans ◽  
Plasma Membrane ◽  
Membrane Protein ◽  
Solute Carrier Family ◽  
Plasma Membrane Protein ◽  
Cellular Functions ◽  
Downstream Target ◽  
Solute Carrier ◽  
High Concentrations

Candida albicans RCH1 (regulator of Ca2+ homoeostasis 1) encodes a protein of ten TM (transmembrane) domains, homologous with human SLC10A7 (solute carrier family 10 member 7), and Rch1p localizes in the plasma membrane. Deletion of RCH1 confers hypersensitivity to high concentrations of extracellular Ca2+ and tolerance to azoles and Li+, which phenocopies the deletion of CaPMC1 (C. albicans PMC1) encoding the vacuolar Ca2+ pump. Additive to CaPMC1 mutation, lack of RCH1 alone shows an increase in Ca2+ sensitivity, Ca2+ uptake and cytosolic Ca2+ level. The Ca2+ hypersensitivity is abolished by cyclosporin A and magnesium. In addition, deletion of RCH1 elevates the expression of CaUTR2 (C. albicans UTR2), a downstream target of the Ca2+/calcineurin signalling. Mutational and functional analysis indicates that the Rch1p TM8 domain, but not the TM9 and TM10 domains, are required for its protein stability, cellular functions and subcellular localization. Therefore Rch1p is a novel regulator of cytosolic Ca2+ homoeostasis, which expands the functional spectrum of the vertebrate SLC10 family.

scholarly journals Expression of solute carrier 7A4 (SLC7A4) in the plasma membrane is not sufficient to mediate amino acid transport activity

2002 ◽  
Vol 364 (3) ◽  
pp. 767-775 ◽  
Author(s):  
Sabine WOLF ◽  
Annette JANZEN ◽  
Nicole VÉKONY ◽  
Ursula MARTINÉ ◽  
Dennis STRAND ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Amino Acid ◽  
Protein Expression ◽  
Amino Acid Transport ◽  
Fluorescent Protein ◽  
Xenopus Laevis Oocytes ◽  
Amino Acid Transporters ◽  
Acid Transport ◽  
Transport Activity ◽  
Solute Carrier

Member 4 of human solute carrier family 7 (SLC7A4) exhibits significant sequence homology with the SLC7 subfamily of human cationic amino acid transporters (hCATs) [Sperandeo, Borsani, Incerti, Zollo, Rossi, Zuffardi, Castaldo, Taglialatela, Andria and Sebastio (1998) Genomics 49, 230–236]. It is therefore often referred to as hCAT-4 even though no convincing transport activity has been shown for this protein. We expressed SLC7A4 in Xenopus laevis oocytes, but could not detect any transport activity for cationic, neutral or anionic amino acids or for the polyamine putrescine. In addition, human glioblastoma cells stably overexpressing a fusion protein between SLC7A4 and the enhanced green fluorescent protein (EGFP) did not exhibit an increased transport activity for l-arginine. The lack of transport activity was not due to a lack of SLC7A4 protein expression in the plasma membrane, as in both cell types SLC7A4-EGFP exhibited a similar subcellular localization and level of protein expression as functional hCAT-EGFP proteins. The expression of SLC7A4 can be induced in NT2 teratocarcinoma cells by treatment with retinoic acid. However, also for this endogenously expressed SLC7A4, we could not detect any transport activity for l-arginine. Our data demonstrate that the expression of SLC7A4 in the plasma membrane is not sufficient to induce an amino acid transport activity in X. laevis oocytes or human cells. Therefore, SLC7A4 is either not an amino acid transporter or it needs additional (protein) factor(s) to be functional.

scholarly journals Epistasis-driven identification of SLC25A51 as a regulator of human mitochondrial NAD import

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Enrico Girardi ◽  
Gennaro Agrimi ◽  
Ulrich Goldmann ◽  
Giuseppe Fiume ◽  
Sabrina Lindinger ◽  
...  
Keyword(s):  
Mitochondrial Respiration ◽  
Genetic Interaction ◽  
Functional Characterization ◽  
Membrane Transporters ◽  
Genetic Interactions ◽  
Functional Information ◽  
Carrier Proteins ◽  
Mitochondrial Import ◽  
Redox Metabolism ◽  
Solute Carrier

AbstractAbout a thousand genes in the human genome encode for membrane transporters. Among these, several solute carrier proteins (SLCs), representing the largest group of transporters, are still orphan and lack functional characterization. We reasoned that assessing genetic interactions among SLCs may be an efficient way to obtain functional information allowing their deorphanization. Here we describe a network of strong genetic interactions indicating a contribution to mitochondrial respiration and redox metabolism for SLC25A51/MCART1, an uncharacterized member of the SLC25 family of transporters. Through a combination of metabolomics, genomics and genetics approaches, we demonstrate a role for SLC25A51 as enabler of mitochondrial import of NAD, showcasing the potential of genetic interaction-driven functional gene deorphanization.

Role and nature of plasma membrane carrier proteins in the hepatic transport of organic anions

1989 ◽  
Vol 4 (2) ◽  
pp. 195-205 ◽  
Author(s):  
CLAUDIO TIRIBELLI ◽  
STEFANO BELLENTANI ◽  
GIAN CARLO LUNAZZI ◽  
GIAN LUIGI SOTTOCASA
Keyword(s):  
Plasma Membrane ◽  
Organic Anions ◽  
Carrier Proteins ◽  
Hepatic Transport

scholarly journals Detection of Chemical Engagement of Solute Carrier Proteins by a Cellular Thermal Shift Assay

2018 ◽  
Vol 13 (6) ◽  
pp. 1480-1486 ◽  
Author(s):  
Mari Hashimoto ◽  
Enrico Girardi ◽  
Ruth Eichner ◽  
Giulio Superti-Furga
Keyword(s):  
Carrier Proteins ◽  
Thermal Shift Assay ◽  
Solute Carrier ◽  
Cellular Thermal Shift Assay ◽  
Thermal Shift

scholarly journals SLC6 neurotransmitter transporter family (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

2019 ◽  
Vol 2019 (4) ◽  
Author(s):  
Stefan Bröer ◽  
Gary Rudnick
Keyword(s):  
Amino Acids ◽  
Plasma Membrane ◽  
Amino Acid ◽  
Crystal Structures ◽  
Structural Motif ◽  
Solute Carrier Family ◽  
Neurotransmitter Transporter ◽  
Transporter Family ◽  
Bacterial Homolog ◽  
Solute Carrier

Members of the solute carrier family 6 (SLC6) of sodium- and (sometimes chloride-) dependent neurotransmitter transporters [29, 22, 70] are primarily plasma membrane located and may be divided into four subfamilies that transport monoamines, GABA, glycine and neutral amino acids, plus the related bacterial NSS transporters [99]. The members of this superfamily share a structural motif of 10 TM segments that has been observed in crystal structures of the NSS bacterial homolog LeuTAa, a Na+-dependent amino acid transporter from Aquiflex aeolicus [126] and in several other transporter families structurally related to LeuT [45].

scholarly journals Rational Exploration of Fold Atlas for Human Solute Carrier Proteins

2021 ◽  
Author(s):  
Tengyu Xie ◽  
Ximin Chi ◽  
Bangdong Huang ◽  
Fangfei Ye ◽  
Qiang Zhou ◽  
...  
Keyword(s):  
Carrier Proteins ◽  
Solute Carrier
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