6533b85cfe1ef96bd12bcaa5
RESEARCH PRODUCT
Characterization of a Novel Type of Serine/Threonine Kinase That Specifically Phosphorylates the Human Goodpasture Antigen
Samuel NavarroFernando RevertAngel RayaJuan Saussubject
Collagen Type IVMolecular Sequence DataSaccharomyces cerevisiaeProtein Serine-Threonine KinasesMolecular cloningBiologymedicine.disease_causeAutoantigensBiochemistryCell LineAutoimmunitymedicineHumansAmino Acid SequenceCloning MolecularPhosphorylationMolecular BiologyPeptide sequenceCeramide Transfer ProteinSerine/threonine-specific protein kinaseBase SequenceSequence Homology Amino AcidKinaseCell BiologyCeramide transportImmunohistochemistryCell biologyBiochemistryProtein BiosynthesisPhosphorylationCollagendescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1999-04-23 | Journal of Biological Chemistry |