Antibody‐induced dimerization of HARPTPα–EGFR chimera suggests a ligand dependent mechanism of regulation for RPTPα

FEBS Letters

Blanchetot, Christophe¹  den Hertog, Jeroen¹ 

[1] Hubrecht Laboratory, Netherlands Institute for Developmental Biology, Uppsalalaan 8, 3584 CT Utrecht, The Netherlands

关键词: Protein tyrosine phosphatase α;    Dimerization;    Regulation;    Ligand;    Epidermal growth factor receptor;    Crosslinking;   

DOI  :  10.1016/S0014-5793(00)02165-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We developed a system to study the function of the ectodomain of RPTPα, a transmembrane protein-tyrosine phosphatase, by fusing the HA-epitope tagged ectodomain of RPTPα to the transmembrane and intracellular domain of the epidermal growth factor receptor, EGFR, a receptor protein-tyrosine kinase that is activated by dimerization. Although the use of chemical crosslinkers shows that preformed HARPTPα–EGFR dimers exist, bivalent anti-HA-tag antibody activated HARPTPα–EGFR chimeras, suggesting this system may be used to study regulation of dimerization. We used this system to show that newborn calf serum may contain (a) potential ligand(s) for RPTPα. Our results suggest that RPTPα dimerization and thus activity may be affected by ligand binding.

【 授权许可】

Unknown