Histidine domain-protein tyrosine phosphatase interacts with Grb2 and GrpL.
Article Details
- CitationCopy to clipboard
Tanase CA
Histidine domain-protein tyrosine phosphatase interacts with Grb2 and GrpL.
PLoS One. 2010 Dec 15;5(12):e14339. doi: 10.1371/journal.pone.0014339.
- PubMed ID
- 21179510 [ View in PubMed]
- Abstract
BACKGROUND: Histidine domain-protein tyrosine phosphatase (HD-PTP) plays a key role in vesicle trafficking and biogenesis. Although it is a large protein with at least five distinct structural domains, only a few of its interactors are presently known, and the significance of these interactions is largely obscure. METHODOLOGY AND RESULTS: In this study we performed a yeast two-hybrid screening using a human colon cDNA library and found that Grb2 and GrpL are binding partners of HD-PTP. Co-immunoprecipitation, pull-down and immunocytochemistry experiments confirmed the interactions. We also discovered that the central proline-rich and histidine-rich domain of HD-PTP is responsible for these interactions. SIGNIFICANCE: The interaction of HD-PTP with two adapters of the Grb2 family, essential for numerous signaling pathways, suggests that HD-PTP might be important for signaling through a plethora of receptors.