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Characterization of the substrate specificity of the inositol 5-phosphatase SHIP1

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Characterization of the substrate specificity of the inositol 5-phosphatase SHIP1. / Nelson, Nina; Wundenberg, Torsten; Lin, Hongying; Rehbach, Christoph; Horn, Stefan; Windhorst, Sabine; Jücker, Manfred.

In: BIOCHEM BIOPH RES CO, Vol. 524, No. 2, 02.04.2020, p. 366-370.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Nelson, N, Wundenberg, T, Lin, H, Rehbach, C, Horn, S, Windhorst, S & Jücker, M 2020, 'Characterization of the substrate specificity of the inositol 5-phosphatase SHIP1', BIOCHEM BIOPH RES CO, vol. 524, no. 2, pp. 366-370. https://doi.org/10.1016/j.bbrc.2020.01.012

APA

Nelson, N., Wundenberg, T., Lin, H., Rehbach, C., Horn, S., Windhorst, S., & Jücker, M. (2020). Characterization of the substrate specificity of the inositol 5-phosphatase SHIP1. BIOCHEM BIOPH RES CO, 524(2), 366-370. https://doi.org/10.1016/j.bbrc.2020.01.012

Vancouver

Nelson N, Wundenberg T, Lin H, Rehbach C, Horn S, Windhorst S et al. Characterization of the substrate specificity of the inositol 5-phosphatase SHIP1. BIOCHEM BIOPH RES CO. 2020 Apr 2;524(2):366-370. https://doi.org/10.1016/j.bbrc.2020.01.012

Bibtex

@article{02747198717c433b83f133418a7929d0,
title = "Characterization of the substrate specificity of the inositol 5-phosphatase SHIP1",
abstract = "SHIP1 is an inositol 5-phosphatase which is well established for its tumour suppressor potential in leukaemia. Enzymatically, two SHIP1 substrates, PtdIns(3,4,5)P3 and Ins(1,3,4,5)P4 have been identified to date. Additional substrates were found for the homologue SHIP2. In this study, we identified new inositol phosphate (InsP) substrates of SHIP1 by metal dye detection high-performance liquid chromatography and compared the substrate profiles of SHIP1 and SHIP2. We were able to verify Ins(1,3,4,5)P4 as a substrate of SHIP1 and interestingly found Ins(1,2,3,4,5)P5 and Ins(2,3,4,5)P4 to be preferably used as substrates and Ins(1,4,5,6)P4 and Ins(2,4,5,6)P4 to be weak substrates. All of those except Ins(2,3,4,5)P4 are also known substrates of SHIP2 indicating a possible exclusive role of Ins(2,3,4,5)P4 hydrolysis for SHIP1 but not SHIP2 function.",
author = "Nina Nelson and Torsten Wundenberg and Hongying Lin and Christoph Rehbach and Stefan Horn and Sabine Windhorst and Manfred J{\"u}cker",
note = "Copyright {\textcopyright} 2020. Published by Elsevier Inc.",
year = "2020",
month = apr,
day = "2",
doi = "10.1016/j.bbrc.2020.01.012",
language = "English",
volume = "524",
pages = "366--370",
journal = "BIOCHEM BIOPH RES CO",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

RIS

TY - JOUR

T1 - Characterization of the substrate specificity of the inositol 5-phosphatase SHIP1

AU - Nelson, Nina

AU - Wundenberg, Torsten

AU - Lin, Hongying

AU - Rehbach, Christoph

AU - Horn, Stefan

AU - Windhorst, Sabine

AU - Jücker, Manfred

N1 - Copyright © 2020. Published by Elsevier Inc.

PY - 2020/4/2

Y1 - 2020/4/2

N2 - SHIP1 is an inositol 5-phosphatase which is well established for its tumour suppressor potential in leukaemia. Enzymatically, two SHIP1 substrates, PtdIns(3,4,5)P3 and Ins(1,3,4,5)P4 have been identified to date. Additional substrates were found for the homologue SHIP2. In this study, we identified new inositol phosphate (InsP) substrates of SHIP1 by metal dye detection high-performance liquid chromatography and compared the substrate profiles of SHIP1 and SHIP2. We were able to verify Ins(1,3,4,5)P4 as a substrate of SHIP1 and interestingly found Ins(1,2,3,4,5)P5 and Ins(2,3,4,5)P4 to be preferably used as substrates and Ins(1,4,5,6)P4 and Ins(2,4,5,6)P4 to be weak substrates. All of those except Ins(2,3,4,5)P4 are also known substrates of SHIP2 indicating a possible exclusive role of Ins(2,3,4,5)P4 hydrolysis for SHIP1 but not SHIP2 function.

AB - SHIP1 is an inositol 5-phosphatase which is well established for its tumour suppressor potential in leukaemia. Enzymatically, two SHIP1 substrates, PtdIns(3,4,5)P3 and Ins(1,3,4,5)P4 have been identified to date. Additional substrates were found for the homologue SHIP2. In this study, we identified new inositol phosphate (InsP) substrates of SHIP1 by metal dye detection high-performance liquid chromatography and compared the substrate profiles of SHIP1 and SHIP2. We were able to verify Ins(1,3,4,5)P4 as a substrate of SHIP1 and interestingly found Ins(1,2,3,4,5)P5 and Ins(2,3,4,5)P4 to be preferably used as substrates and Ins(1,4,5,6)P4 and Ins(2,4,5,6)P4 to be weak substrates. All of those except Ins(2,3,4,5)P4 are also known substrates of SHIP2 indicating a possible exclusive role of Ins(2,3,4,5)P4 hydrolysis for SHIP1 but not SHIP2 function.

U2 - 10.1016/j.bbrc.2020.01.012

DO - 10.1016/j.bbrc.2020.01.012

M3 - SCORING: Journal article

C2 - 32005521

VL - 524

SP - 366

EP - 370

JO - BIOCHEM BIOPH RES CO

JF - BIOCHEM BIOPH RES CO

SN - 0006-291X

IS - 2

ER -