Characterization of a novel type of serine/threonine kinase that specifically phosphorylates the human goodpasture antigen

J Biol Chem. 1999 Apr 30;274(18):12642-9. doi: 10.1074/jbc.274.18.12642.

Abstract

Goodpasture disease is an autoimmune disorder that occurs naturally only in humans. Also exclusive to humans is the phosphorylation process that targets the unique N-terminal region of the Goodpasture antigen. Here we report the molecular cloning of GPBP (Goodpasture antigen-binding protein), a previously unknown 624-residue polypeptide. Although the predicted sequence does not meet the conventional structural requirements for a protein kinase, its recombinant counterpart specifically binds to and phosphorylates the exclusive N-terminal region of the human Goodpasture antigen in vitro. This novel kinase is widely expressed in human tissues but shows preferential expression in the histological structures that are targets of common autoimmune responses. The work presented in this report highlights a novel gene to be explored in human autoimmunity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Autoantigens / chemistry
  • Autoantigens / metabolism*
  • Base Sequence
  • Cell Line
  • Cloning, Molecular
  • Collagen / chemistry
  • Collagen / metabolism*
  • Collagen Type IV*
  • Humans
  • Immunohistochemistry
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Biosynthesis
  • Protein Serine-Threonine Kinases / chemistry
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*
  • Saccharomyces cerevisiae / genetics
  • Sequence Homology, Amino Acid

Substances

  • Autoantigens
  • Collagen Type IV
  • type IV collagen alpha3 chain
  • Collagen
  • CERT1 protein, human
  • Protein Serine-Threonine Kinases

Associated data

  • GENBANK/AF136450