A protocol for the production of KLRG1 tetramer.

J Vis Exp

Department of Molecular Microbiology and Immunology, Brown University, USA.

Published: January 2010

AI Article Synopsis

  • KLRG1 is an inhibitory receptor found on mature NK and certain T cells, important for immune response regulation.
  • It exists as both a monomer and a homodimer, and interacts with cadherins, which are key for cell adhesion and communication.
  • The creation of the KLRG1 tetramer was crucial for identifying these interactions and understanding the broader implications for immune function and tissue maintenance.

Article Abstract

Killer cell lectin-like receptor G1 (KLRG1) is a type II transmembrane glycoprotein inhibitory receptor belonging to the C type lectin-like superfamily. KLRG1 exists both as a monomer and as a disulfide-linked homodimer. This well-conserved receptor is found on the most mature and recently activated NK cells as well as on a subset of effector/memory T cells. Using KLRG1 tetramer as well as other methods, E-, N-, and R-cadherins were identified as KLRG1 ligands. These Ca(2+)-dependent cell-cell adhesion molecules comprises of an extracellular domain containing five cadherin repeats responsible for cell-cell interactions, a transmembrane domain and a cytoplasmic domain that is linked to the actin cytoskeleton. Generation of the KLRG1 tetramer was essential to the identification of the KLRG1 ligands. KLRG1 tetramer is also a unique tool to elucidate the roles cadherin and KLRG1 play in regulating the immune response and tissue integrity.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2848686PMC
http://dx.doi.org/10.3791/1701DOI Listing

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