Rush Hour of LATs towards Their Transport Cycle
The mammalian SLC7 family comprises the L-amino acid transporters (LATs) and the cationic amino acid transporters (CATs). The relevance of these transporters is highlighted by their involvement in several human pathologies, including inherited rare diseases and acquired diseases, such as cancer. In...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-08-01
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| Series: | Membranes |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2077-0375/11/8/602 |
| _version_ | 1797522972581298176 |
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| author | Adrià Nicolàs-Aragó Joana Fort Manuel Palacín Ekaitz Errasti-Murugarren |
| author_facet | Adrià Nicolàs-Aragó Joana Fort Manuel Palacín Ekaitz Errasti-Murugarren |
| author_sort | Adrià Nicolàs-Aragó |
| collection | DOAJ |
| description | The mammalian SLC7 family comprises the L-amino acid transporters (LATs) and the cationic amino acid transporters (CATs). The relevance of these transporters is highlighted by their involvement in several human pathologies, including inherited rare diseases and acquired diseases, such as cancer. In the last four years, several crystal or cryo-EM structures of LATs and CATs have been solved. These structures have started to fill our knowledge gap that previously was based on the structural biology of remote homologs of the amino acid–polyamine–organocation (APC) transporters. This review recovers this structural and functional information to start generating the molecular bases of the transport cycle of LATs. Special attention is given to the known transporter conformations within the transport cycle and the molecular bases for substrate interaction and translocation, including the asymmetric interaction of substrates at both sides of the plasma membrane. |
| first_indexed | 2024-03-10T08:35:59Z |
| format | Article |
| id | doaj.art-34510d7bda9e4441916038411570b465 |
| institution | Directory Open Access Journal |
| issn | 2077-0375 |
| language | English |
| last_indexed | 2024-03-10T08:35:59Z |
| publishDate | 2021-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Membranes |
| spelling | doaj.art-34510d7bda9e4441916038411570b4652023-11-22T08:38:03ZengMDPI AGMembranes2077-03752021-08-0111860210.3390/membranes11080602Rush Hour of LATs towards Their Transport CycleAdrià Nicolàs-Aragó0Joana Fort1Manuel Palacín2Ekaitz Errasti-Murugarren3Laboratory of Amino Acid Transporters and Disease, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST), Baldiri Reixac 10, 08028 Barcelona, SpainLaboratory of Amino Acid Transporters and Disease, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST), Baldiri Reixac 10, 08028 Barcelona, SpainLaboratory of Amino Acid Transporters and Disease, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST), Baldiri Reixac 10, 08028 Barcelona, SpainLaboratory of Amino Acid Transporters and Disease, Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology (BIST), Baldiri Reixac 10, 08028 Barcelona, SpainThe mammalian SLC7 family comprises the L-amino acid transporters (LATs) and the cationic amino acid transporters (CATs). The relevance of these transporters is highlighted by their involvement in several human pathologies, including inherited rare diseases and acquired diseases, such as cancer. In the last four years, several crystal or cryo-EM structures of LATs and CATs have been solved. These structures have started to fill our knowledge gap that previously was based on the structural biology of remote homologs of the amino acid–polyamine–organocation (APC) transporters. This review recovers this structural and functional information to start generating the molecular bases of the transport cycle of LATs. Special attention is given to the known transporter conformations within the transport cycle and the molecular bases for substrate interaction and translocation, including the asymmetric interaction of substrates at both sides of the plasma membrane.https://www.mdpi.com/2077-0375/11/8/602APCLATsSLC7transport cyclestructuresubstrate binding |
| spellingShingle | Adrià Nicolàs-Aragó Joana Fort Manuel Palacín Ekaitz Errasti-Murugarren Rush Hour of LATs towards Their Transport Cycle Membranes APC LATs SLC7 transport cycle structure substrate binding |
| title | Rush Hour of LATs towards Their Transport Cycle |
| title_full | Rush Hour of LATs towards Their Transport Cycle |
| title_fullStr | Rush Hour of LATs towards Their Transport Cycle |
| title_full_unstemmed | Rush Hour of LATs towards Their Transport Cycle |
| title_short | Rush Hour of LATs towards Their Transport Cycle |
| title_sort | rush hour of lats towards their transport cycle |
| topic | APC LATs SLC7 transport cycle structure substrate binding |
| url | https://www.mdpi.com/2077-0375/11/8/602 |
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