4.5 Review

Rush Hour of LATs towards Their Transport Cycle

Journal

MEMBRANES
Volume 11, Issue 8, Pages -

Publisher

MDPI
DOI: 10.3390/membranes11080602

Keywords

APC; LATs; SLC7; transport cycle; structure; substrate binding; substrate translocation

Funding

  1. Spanish Ministry of Science, Innovation and Universities (MSIU) [SAF2015-64869-R-FEDER, RTI2018-094211-B-I00]
  2. Fundacio La Marato-TV3
  3. La Caixa Health Research [LCF/PR/HR20/52400017]
  4. MSIU

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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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