histidine domain-protein tyrosine phosphatase interacts with grb2 and grpl组氨酸domain-protein酪氨酸磷酸酶与grb2和grpl交互.pdfVIP
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histidine domain-protein tyrosine phosphatase interacts with grb2 and grpl组氨酸domain-protein酪氨酸磷酸酶与grb2和grpl交互
Histidine Domain-Protein Tyrosine Phosphatase Interacts
with Grb2 and GrpL
Carmen-Alexandra Tanase*
Department of Enzymology, Institute of Biochemistry, Bucharest, Romania
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.
Citation: Tanase C-A (2010) Histidine Domain-Protein Tyrosine Phosphatase Interacts with Grb2 and GrpL. PLoS ONE 5(12): e14339. doi:10.1371/
journal.pone.0014339
Editor: Guillaume Dalmasso, Emory Unviersity, United States of America
Received July 14, 2010; Accepted November 25, 2010; Published December 15, 2010
Copyright: 2010 Carmen-Alexandra Tanase. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which
permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Funding: This work was supported by a grant from the Romanian Council for Research and Higher Education (grant number 3182) and by a Marie Curie
International Reintegration Gra
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