| Title |
The ancillary proteins of HATs: SLC3 family of amino acid transporters
|
|---|---|
| Published in |
Pflügers Archiv - European Journal of Physiology, May 2003
|
| DOI | 10.1007/s00424-003-1062-7 |
| Pubmed ID | |
| Authors |
Manuel Palacín, Yoshikatsu Kanai |
| Abstract |
The heteromeric amino acid transporters (HATs) are composed of a light and a heavy subunit linked by a disulfide bridge. The heavy subunits are the SLC3 members (rBAT and 4F2hc), whereas the light subunits are members of the SLC7 family of amino acid transporters. SLC3 proteins are type II membrane glycoproteins (i.e., one single transmembrane domain and the C-terminus located outside the cell) with a bulky extracellular domain that shows homology with alpha-glucosidases. rBAT heterodimerizes with b(0,+)AT (SLC7A9) constituting the amino acid transport b(0,+), the main system responsible for the apical reabsorption of cystine in kidney. The defect in this system causes cystinuria, the most common primary inherited aminoaciduria. 4F2hc subserves various amino acid transport systems by dimerization with different SLC7 proteins. The main role of SLC3 proteins is to help routing of the holotransporter to the plasma membrane. A working model for the biogenesis of HATs based on recent data on the rBAT/b(0,+)AT heterodimeric complex is presented. 4F2hc is a multifunctional protein, and in addition to its role in amino acid transport, it may be involved in other cellular functions. Studies on two SLC7 members (Asc-2 and AGT1) demonstrate heterodimerization with unknown heavy subunits. |
Mendeley readers
The data shown below were compiled from readership statistics for 75 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| United States | 2 | 3% |
| United Kingdom | 1 | 1% |
| Brazil | 1 | 1% |
| Unknown | 71 | 95% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Researcher | 18 | 24% |
| Student > Ph. D. Student | 14 | 19% |
| Student > Master | 10 | 13% |
| Professor > Associate Professor | 7 | 9% |
| Student > Doctoral Student | 5 | 7% |
| Other | 12 | 16% |
| Unknown | 9 | 12% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 29 | 39% |
| Biochemistry, Genetics and Molecular Biology | 18 | 24% |
| Chemistry | 5 | 7% |
| Medicine and Dentistry | 4 | 5% |
| Pharmacology, Toxicology and Pharmaceutical Science | 3 | 4% |
| Other | 7 | 9% |
| Unknown | 9 | 12% |
Attention Score in Context
This research output has an Altmetric Attention Score of 3. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 03 July 2022.
All research outputs
#8,535,472
of 25,374,647 outputs
Outputs from Pflügers Archiv - European Journal of Physiology
#513
of 2,055 outputs
Outputs of similar age
#18,794
of 54,766 outputs
Outputs of similar age from Pflügers Archiv - European Journal of Physiology
#18
of 29 outputs
Altmetric has tracked 25,374,647 research outputs across all sources so far. This one is in the 43rd percentile – i.e., 43% of other outputs scored the same or lower than it.
So far Altmetric has tracked 2,055 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 5.1. This one is in the 41st percentile – i.e., 41% of its peers scored the same or lower than it.
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We're also able to compare this research output to 29 others from the same source and published within six weeks on either side of this one. This one is in the 6th percentile – i.e., 6% of its contemporaries scored the same or lower than it.