hd-ptp is a catalytically inactive tyrosine phosphatase due to a conserved divergence in its phosphatase domainhd-ptp是催化地不活跃的酪氨酸磷酸酶由于守恒的散度的磷酸酶域.pdfVIP
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hd-ptp is a catalytically inactive tyrosine phosphatase due to a conserved divergence in its phosphatase domainhd-ptp是催化地不活跃的酪氨酸磷酸酶由于守恒的散度的磷酸酶域
HD-PTP Is a Catalytically Inactive Tyrosine Phosphatase
Due to a Conserved Divergence in Its Phosphatase
Domain
1 1 1 2 2
Marie-Claude Gingras , Yu Ling Zhang , Dmitri Kharitidi , Alastair J. Barr , Stefan Knapp , Michel L.
1 1
Tremblay , Arnim Pause *
´ ´
1 Goodman Cancer Centre and Department of Biochemistry, McGill University, Montreal, Quebec, Canada, 2 Structural Genomics Consortium, Nuffield Department of
Medicine, University of Oxford, Oxford, United Kingdom
Abstract
Background: The HD-PTP protein has been described as a tumor suppressor candidate and based on its amino acid
sequence, categorized as a classical non-transmembrane protein tyrosine phosphatase (PTP). To date, no HD-PTP
phosphorylated substrate has been identified and controversial results concerning its catalytic activity have been recently
reported.
Methodology and Results: Here we report a rigorous enzymatic analysis demonstrating that the HD-PTP protein does not
harbor tyrosine phosphatase or lipid phosphatase activity using the highly sensitive DiFMUP substrate and a panel of
different phosphatidylinositol phosphates. We found that HD-PTP tyrosine phosphatase inactivity is caused by an
evolutionary conserved amino acid divergence of a key residue located in the HD-PTP phosphatase domain since its back
mutation is sufficient to restore the HD-PTP tyrosine phosphatase activity. Moreover, in agreement with a tumor suppressor
activity, HD-PTP expression leads to colony growth reduction in human cancer cell lines, independently of its catalytic
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