期刊
MEMBRANES
卷 11, 期 8, 页码 -出版社
MDPI
DOI: 10.3390/membranes11080602
关键词
APC; LATs; SLC7; transport cycle; structure; substrate binding; substrate translocation
类别
资金
- Spanish Ministry of Science, Innovation and Universities (MSIU) [SAF2015-64869-R-FEDER, RTI2018-094211-B-I00]
- Fundacio La Marato-TV3
- La Caixa Health Research [LCF/PR/HR20/52400017]
- MSIU
The mammalian SLC7 family consists of LATs and CATs, which are involved in various human pathologies. Recent structural studies have provided insights into the molecular basis of the transport cycle of LATs. This review focuses on the structural and functional information of LATs to understand substrate interaction and translocation.
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.
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