Molecular characterization of two novel alternative spliced variants of the KLRF1 gene and subcellular distribution of KLRF1 isoforms

Biochim Biophys Acta. 2001 Aug 30;1520(2):141-6. doi: 10.1016/s0167-4781(01)00261-5.

Abstract

The killer cell lectin-like receptor (KLR) family is formed by type II transmembrane glycoproteins with a single extracellular C-type lectin-like domain (CTLD). Some of these glycoproteins are involved in the regulation of natural killer cell activity. Recently, we have described the molecular characterization of the KLRF1 gene and the existence of one alternative spliced form, lacking the stalk region of the extracellular domain. In this work we describe two novel KLRF1 alternative spliced variants coding for truncated proteins lacking the CTLD. In addition, we present the biochemical analysis of the KLRF1 protein and the subcellular distribution of all KLRF1 isoforms expressed in heterologous transfectants.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alternative Splicing
  • Amino Acid Sequence
  • Cell Line
  • Cell Membrane / chemistry
  • Cytoplasm / chemistry
  • DNA, Complementary / chemistry
  • Lectins*
  • Lectins, C-Type
  • Microscopy, Confocal
  • Molecular Sequence Data
  • Plasmids
  • Protein Isoforms / biosynthesis
  • Protein Isoforms / chemistry
  • Protein Isoforms / genetics
  • RNA / chemistry
  • Receptors, Immunologic / chemistry
  • Receptors, Immunologic / genetics*
  • Receptors, Natural Killer Cell
  • Reverse Transcriptase Polymerase Chain Reaction
  • Transfection

Substances

  • DNA, Complementary
  • KLRF1 protein, human
  • Lectins
  • Lectins, C-Type
  • Protein Isoforms
  • Receptors, Immunologic
  • Receptors, Natural Killer Cell
  • RNA

Associated data

  • GENBANK/AF267244
  • GENBANK/AF267245