ⓘ Galectin-8

                                     

ⓘ Galectin-8

This gene encodes a member of the galectin family. Galectins are beta-galactoside-binding animal lectins with conserved carbohydrate recognition domains. The galectins have been implicated in many essential functions including development, differentiation, cell-cell adhesion, cell-matrix interaction, growth regulation, apoptosis, and RNA splicing. This gene is widely expressed in tumoral tissues and seems to be involved in integrin-like cell interactions. Alternatively spliced transcript variants encoding different isoforms have been identified.

Galectin-8, interacts with the regulatory systems of mTOR in the composition SLC38A9, Ragulator, Ragab, RagCD. Galectin-8 control of mTOR leads to its inactivation and dissociation from damaged lysosomes, therefore transformations that a violation of lysosomal membranes on mTOR. Physiological consequences of inhibition of mTOR following damage to lysosomal membranes cover of autophagy and metabolic shift.

                                     
  • peptide domain. Tandem galectins include galectin - 4, - 6, - 8 - 9 and - 12. The final galectin is galectin - 3 which is the only galectin found in the chimera
  • Galectin - 3 is a protein that in humans is encoded by the LGALS3 gene. Galectin - 3 is a member of the lectin family, of which 14 mammalian galectins have
  • Galectin - 4 is a protein that in humans is encoded by the LGALS4 gene. The galectins are a family of beta - galactoside - binding proteins implicated in modulating
  • Galectin - 1 is a protein that in humans is encoded by the LGALS1 gene. LGALS1 contains four exons. The galectin - 1 protein is 135 amino acids in length and
  • Galectin - 9 was first time isolated from mouse embryonic kidney in 1997 as a 36 kDa beta - galactoside lectin protein. Human galectin - 9 is encoded by the
  • Galectin - 2 is a protein that in humans is encoded by the LGALS2 gene. The protein encoded by this gene is a soluble beta - galactoside binding lectin. The
  • autophagy. He discovered a new pathway of cell - autonomous defence relying on galectin - 8 as the receptor for membrane - damage caused by cytosol - invading bacteria
  • binding site is lack of key residue for binding beta - galactoside. It is a galectin - like protein. The ligand of this protein is still unknown. PP13 levels
  • Cell, this group has shown that a novel system termed GALTOR, based on Galectin - 8 interacts with the mTOR regulatory system composed of SLC38A9, Ragulator