Molecular physiology of the insect K-activated amino acid transporter 1 (KAAT1) and cation-anion activated amino acid transporter/channel 1 (CAATCH1) in the light of the structure of the homologous protein LeuT

Insect Mol Biol. 2009 Jun;18(3):265-79. doi: 10.1111/j.1365-2583.2009.00881.x. Epub 2009 Apr 6.

Abstract

K-activated amino acid transporter 1 (KAAT1) and cation-anion-activated amino acid transporter/channel 1 (CAATCH1) are amino acid cotransporters, belonging to the Na/Cl-dependent neurotransmitter transporter family (also called SLC6/NSS), that have been cloned from Manduca sexta midgut. They have been thoroughly studied by expression in Xenopus laevis oocytes, and structure/function analyses have made it possible to identify the structural determinants of their cation and amino acid selectivity. About 40 mutants of these proteins have been studied by measuring amino acid uptake and current/voltage relationships. The results obtained since the cloning of KAAT1 and CAATCH1 are here discussed in the light of the 3D model of the first crystallized member of the family, the leucine transporter LeuT.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Transport Systems, Neutral / chemistry
  • Amino Acid Transport Systems, Neutral / metabolism*
  • Animals
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism*
  • Insect Proteins / chemistry
  • Insect Proteins / metabolism*
  • Manduca / metabolism*
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Oocytes
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship
  • Xenopus laevis

Substances

  • Amino Acid Transport Systems, Neutral
  • CAATCH1 protein, insect
  • Carrier Proteins
  • Insect Proteins
  • KAAT1 protein, insect
  • Membrane Proteins