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PLoS One. 2010 Dec 15;5(12):e14339. doi: 10.1371/journal.pone.0014339.

Histidine domain-protein tyrosine phosphatase interacts with Grb2 and GrpL.

Author information

  • Department of Enzymology, Institute of Biochemistry, Bucharest, Romania. ctanase@biochim.ro

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.

PMID:
21179510
[PubMed - indexed for MEDLINE]
PMCID:
PMC3002266
Free PMC Article

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