scholarly journals Amino Acid Transporters in Plants: Identification and Function

Plants ◽  
2020 ◽  
Vol 9 (8) ◽  
pp. 972
Author(s):  
Xuehui Yao ◽  
Jing Nie ◽  
Ruoxue Bai ◽  
Xiaolei Sui
Keyword(s):  
Amino Acid ◽  
Agricultural Production ◽  
Carbon Assimilation ◽  
Phloem Loading ◽  
Amino Acid Transporters ◽  
Molecular Identity ◽  
Current State ◽  
Loading And Unloading ◽  
Phloem Loading And Unloading ◽  
And Function

Amino acid transporters are the main mediators of nitrogen distribution throughout the plant body, and are essential for sustaining growth and development. In this review, we summarize the current state of knowledge on the identity and biological functions of amino acid transporters in plants, and discuss the regulation of amino acid transporters in response to environmental stimuli. We focus on transporter function in amino acid assimilation and phloem loading and unloading, as well as on the molecular identity of amino acid exporters. Moreover, we discuss the effects of amino acid transport on carbon assimilation, as well as their cross-regulation, which is at the heart of sustainable agricultural production.

scholarly journals Amino Acid Transporters in Plant Cells: A Brief Review

Plants ◽  
2020 ◽  
Vol 9 (8) ◽  
pp. 967
Author(s):  
Guangzhe Yang ◽  
Qiuxing Wei ◽  
Hao Huang ◽  
Jixing Xia
Keyword(s):  
Amino Acid ◽  
Intracellular Transport ◽  
Abiotic Stress Tolerance ◽  
Amino Acid Uptake ◽  
Phloem Loading ◽  
Amino Acid Transporters ◽  
Acid Uptake ◽  
Potential Applications ◽  
Phloem Loading And Unloading ◽  
Development Regulation

Amino acids are not only a nitrogen source that can be directly absorbed by plants, but also the major transport form of organic nitrogen in plants. A large number of amino acid transporters have been identified in different plant species. Despite belonging to different families, these amino acid transporters usually exhibit some general features, such as broad expression pattern and substrate selectivity. This review mainly focuses on transporters involved in amino acid uptake, phloem loading and unloading, xylem-phloem transfer, import into seed and intracellular transport in plants. We summarize the other physiological roles mediated by amino acid transporters, including development regulation, abiotic stress tolerance and defense response. Finally, we discuss the potential applications of amino acid transporters for crop genetic improvement.

scholarly journals Pichia pastoris and the Recombinant Human Heterodimeric Amino Acid Transporter 4F2hc-LAT1: From Clone Selection to Pure Protein

2021 ◽  
Vol 4 (3) ◽  
pp. 51
Author(s):  
Satish Kantipudi ◽  
Daniel Harder ◽  
Sara Bonetti ◽  
Dimitrios Fotiadis ◽  
Jean-Marc Jeckelmann
Keyword(s):  
Amino Acid ◽  
Pichia Pastoris ◽  
Protein Complexes ◽  
Amino Acid Transporter ◽  
Amino Acid Transporters ◽  
Expression Host ◽  
Amino Acids And Derivatives ◽  
Heterodimeric Complex ◽  
Acid Transporter ◽  
And Function

Heterodimeric amino acid transporters (HATs) are protein complexes composed of two subunits, a heavy and a light subunit belonging to the solute carrier (SLC) families SLC3 and SLC7. HATs transport amino acids and derivatives thereof across the plasma membrane. The human HAT 4F2hc-LAT1 is composed of the type-II membrane N-glycoprotein 4F2hc (SLC3A2) and the L-type amino acid transporter LAT1 (SLC7A5). 4F2hc-LAT1 is medically relevant, and its dysfunction and overexpression are associated with autism and tumor progression. Here, we provide a general applicable protocol on how to screen for the best membrane transport protein-expressing clone in terms of protein amount and function using Pichia pastoris as expression host. Furthermore, we describe an overexpression and purification procedure for the production of the HAT 4F2hc-LAT1. The isolated heterodimeric complex is pure, correctly assembled, stable, binds the substrate L-leucine, and is thus properly folded. Therefore, this Pichia pastoris-derived recombinant human 4F2hc-LAT1 sample can be used for downstream biochemical and biophysical characterizations.

scholarly journals Recent Advance in the Relationship between Excitatory Amino Acid Transporters and Parkinson’s Disease

2016 ◽  
Vol 2016 ◽  
pp. 1-8 ◽  
Author(s):  
Yunlong Zhang ◽  
Feng Tan ◽  
Pingyi Xu ◽  
Shaogang Qu
Keyword(s):  
Parkinson’S Disease ◽  
Amino Acid ◽  
Animal Models ◽  
Substantia Nigra ◽  
Excitatory Amino Acid ◽  
Synaptic Cleft ◽  
Dopamine Neurons ◽  
Amino Acid Transporters ◽  
Excitatory Amino Acid Transporters ◽  
And Function

Parkinson’s disease (PD) is the most common movement disorder disease in the elderly and is characterized by degeneration of dopamine neurons and formation of Lewy bodies. Glutamate is the major excitatory neurotransmitter in the central nervous system (CNS). If glutamate is not removed promptly in the synaptic cleft, it will excessively stimulate the glutamate receptors and induce excitotoxic effects on the CNS. With lack of extracellular enzyme to decompose glutamate, glutamate uptake in the synaptic cleft is mainly achieved by the excitatory amino acid transporters (EAATs, also known as high-affinity glutamate transporters). Current studies have confirmed that decreased expression and function of EAATs appear in PD animal models. Moreover, single unilateral administration of EAATs inhibitor in the substantia nigra mimics several PD features and this is a solid evidence supporting that decreased EAATs contribute to the process of PD. Drugs or treatments promoting the expression and function of EAATs are shown to attenuate dopamine neurons death in the substantia nigra and striatum, ameliorate the behavior disorder, and improve cognitive abilities in PD animal models. EAATs are potential effective drug targets in treatment of PD and thus study of relationship between EAATs and PD has predominant medical significance currently.

Structure and Function of Cationic Amino Acid Transporters (CATs)

2006 ◽  
Vol 213 (2) ◽  
pp. 67-77 ◽  
Author(s):  
E.I. Closs ◽  
J.-P. Boissel ◽  
A. Habermeier ◽  
A. Rotmann
Keyword(s):  
Amino Acid ◽  
Structure And Function ◽  
Amino Acid Transporters ◽  
Cationic Amino Acid ◽  
And Function

scholarly journals Phloem loading and unloading of Cowpea mosaic virus in Vigna unguiculata

2002 ◽  
Vol 83 (6) ◽  
pp. 1493-1504 ◽  
Author(s):  
M. S. Silva ◽  
J. Wellink ◽  
R. W. Goldbach ◽  
J. W. M. van Lent
Keyword(s):  
Mosaic Virus ◽  
Vigna Unguiculata ◽  
Cell Movement ◽  
Cell Types ◽  
Phloem Loading ◽  
Cowpea Mosaic Virus ◽  
Class Iii ◽  
Long Distance ◽  
Loading And Unloading ◽  
Phloem Loading And Unloading

Within their host plants, viruses spread from the initially infected cell through plasmodesmata to neighbouring cells (cell-to-cell movement), until reaching the phloem for rapid invasion of the younger plant parts (long-distance or vascular movement). Cowpea mosaic virus (CPMV) moves from cell-to-cell as mature virions via tubules constructed of the viral movement protein (MP). The mechanism of vascular movement, however, is not well understood. The characteristics of vascular movement of CPMV in Vigna unguiculata (cowpea) were examined using GFP-expressing recombinant viruses. It was established that CPMV was loaded into both major and minor veins of the inoculated primary leaf, but was unloaded exclusively from major veins, preferably class III, in cowpea trifoliate leaves. Phloem loading and unloading of CPMV was scrutinized at the cellular level in sections of loading and unloading veins. At both loading and unloading sites it was shown that the virus established infection in all vascular cell types with the exception of companion cells (CC) and sieve elements (SE). Furthermore tubular structures, indicative of virion movement, were never found in plasmodesmata connecting phloem parenchyma cells and CC or CC and SE. In cowpea, SE are symplasmically connected only to the CC and these results therefore suggest that CPMV employs a mechanism for phloem loading and unloading that is different from the typical tubule-guided cell-to-cell movement in other cell types.

Sign in / Sign up

Export Citation Format

Share Document