Evidence map›Paper›PMID 33417224›Full record

ArticleMolecular neurobiology2021

Dual-Specificity Phosphatase 15 (DUSP15) Modulates Notch Signaling by Enhancing the Stability of Notch Protein.

Noopur Bhore, Bo-Jeng Wang, Po-Fan Wu, Yen-Lurk Lee, Yun-Wen Chen, Wen-Ming Hsu, Hsinyu Lee, Yi-Shuian Huang, Ding-I Yang, Yung-Feng Liao

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Article in Molecular neurobiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 53% of its field
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed, 3 citations in OpenAlex.

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4 · The record

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5 · Who and what money

Authors and funding

10 authors at 4 institutions in 1 country.

Noopur BhoreLaboratory of Molecular Neurobiology, Institute of Cellular and Organismic Biology, Academia Sinica, ICOB 238, 128 Sec. 2 Academia Rd, Taipei, 11529, Taiwan.
Bo-Jeng WangLaboratory of Molecular Neurobiology, Institute of Cellular and Organismic Biology, Academia Sinica, ICOB 238, 128 Sec. 2 Academia Rd, Taipei, 11529, Taiwan.
Po-Fan WuLaboratory of Molecular Neurobiology, Institute of Cellular and Organismic Biology, Academia Sinica, ICOB 238, 128 Sec. 2 Academia Rd, Taipei, 11529, Taiwan.
Yen-Lurk LeeTIGP in Molecular Medicine, National Yang-Ming University, Academia Sinica, Taipei, Taiwan.
Yun-Wen ChenLaboratory of Molecular Neurobiology, Institute of Cellular and Organismic Biology, Academia Sinica, ICOB 238, 128 Sec. 2 Academia Rd, Taipei, 11529, Taiwan.
Wen-Ming HsuDepartment of Surgery, National Taiwan University Hospital, National Taiwan University College of Medicine, Taipei, Taiwan.
Hsinyu LeeDepartment of Life Science, National Taiwan University, Taipei, Taiwan.
Yi-Shuian HuangTaiwan International Graduate Program in Interdisciplinary Neuroscience, National Yang-Ming University, Academia Sinica, Taipei, Taiwan.
Ding-I YangTaiwan International Graduate Program in Interdisciplinary Neuroscience, National Yang-Ming University, Academia Sinica, Taipei, Taiwan.
Yung-Feng LiaoLaboratory of Molecular Neurobiology, Institute of Cellular and Organismic Biology, Academia Sinica, ICOB 238, 128 Sec. 2 Academia Rd, Taipei, 11529, Taiwan. yliao@sinica.edu.tw.ORCID http://orcid.org/0000-0002-7379-9402
National Yang Ming Chiao Tung University · TWInstitute of Cellular and Organismic Biology, Academia Sinica · TWNational Taiwan University · TWNational Taiwan University Hospital · TW

Funding

Academia Sinica AS-SUMMIT-108Ministry of Science and Technology, Taiwan MOST 107-0210-01-19-01Ministry of Science and Technology, Taiwan MOST 107-2320-B-001-019Ministry of Science and Technology, Taiwan MOST 108-2320-B-001-009Ministry of Science and Technology, Taiwan MOST 108-3114-Y-001-002Ministry of Science and Technology, Taiwan MOST 109-2320-B-001-016The Program for Translational Innovation of Biopharmaceutical Development - Technology Supporting Platform Axis AS-KPQ-106-TSPA
6 · The paper itself

Abstract

Dual-specificity phosphatases (DUSPs) comprise a unique group of enzymes that dephosphorylate signaling proteins at both phospho-serine/threonine and phospho-tyrosine residues. Since Notch signaling is an essential pathway for neuronal cell fate determination and development that is also upregulated in Alzheimer's disease tissues, we sought to explore whether and how DUSPs may impact Notch processing. Our results show that overexpression of DUSP15 concomitantly and dose-dependently increased the steady-state levels of recombinant Notch (extracellular domain-truncated Notch, NotchΔE) protein and its cleaved product, Notch intracellular domain (NICD). The overall ratio of NotchΔE to NICD was unchanged by overexpression of DUSP15, suggesting that the effect is independent of γ-secretase. Interestingly, overexpression of DUSP15 also dose-dependently increased phosphorylated ERK1/2. Phosphorylated ERK1/2 is known to be positively correlated with Notch protein level, and we found that DUSP15-mediated regulation of Notch was dependent on ERK1/2 activity. Together, our findings reveal the existence of a previously unidentified DUSP15-ERK1/2-Notch signaling axis, which could potentially play a role in neuronal differentiation and neurological disease.

Indexed as

Amyloid Precursor Protein SecretasesCell DifferentiationDual-Specificity PhosphatasesHEK293 CellsHumansNeuronsPhosphorylationReceptors, NotchSignal TransductionAmyloid Precursor Protein SecretasesDual-Specificity PhosphatasesDUSP15 protein, humanReceptors, NotchDual-specificity phosphatasesERK1/2Neuronal differentiationNotchPresenilin-1

Identifiers

PMID33417224
OpenAlexW3118580772

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.