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KANPHOS: A Database of Kinase-Associated Neural Protein Phosphorylation in the Brain
Protein phosphorylation plays critical roles in a variety of intracellular signaling pathways and physiological functions that are controlled by neurotransmitters and neuromodulators in the brain. Dysregulation of these signaling pathways has been implicated in neurodevelopmental disorders, includin...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8750479/ https://www.ncbi.nlm.nih.gov/pubmed/35011609 http://dx.doi.org/10.3390/cells11010047 |
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author | Ahammad, Rijwan Uddin Nishioka, Tomoki Yoshimoto, Junichiro Kannon, Takayuki Amano, Mutsuki Funahashi, Yasuhiro Tsuboi, Daisuke Faruk, Md. Omar Yamahashi, Yukie Yamada, Kiyofumi Nagai, Taku Kaibuchi, Kozo |
author_facet | Ahammad, Rijwan Uddin Nishioka, Tomoki Yoshimoto, Junichiro Kannon, Takayuki Amano, Mutsuki Funahashi, Yasuhiro Tsuboi, Daisuke Faruk, Md. Omar Yamahashi, Yukie Yamada, Kiyofumi Nagai, Taku Kaibuchi, Kozo |
author_sort | Ahammad, Rijwan Uddin |
collection | PubMed |
description | Protein phosphorylation plays critical roles in a variety of intracellular signaling pathways and physiological functions that are controlled by neurotransmitters and neuromodulators in the brain. Dysregulation of these signaling pathways has been implicated in neurodevelopmental disorders, including autism spectrum disorder, attention deficit hyperactivity disorder and schizophrenia. While recent advances in mass spectrometry-based proteomics have allowed us to identify approximately 280,000 phosphorylation sites, it remains largely unknown which sites are phosphorylated by which kinases. To overcome this issue, previously, we developed methods for comprehensive screening of the target substrates of given kinases, such as PKA and Rho-kinase, upon stimulation by extracellular signals and identified many candidate substrates for specific kinases and their phosphorylation sites. Here, we developed a novel online database to provide information about the phosphorylation signals identified by our methods, as well as those previously reported in the literature. The “KANPHOS” (Kinase-Associated Neural Phospho-Signaling) database and its web portal were built based on a next-generation XooNIps neuroinformatics tool. To explore the functionality of the KANPHOS database, we obtained phosphoproteomics data for adenosine-A2A-receptor signaling and its downstream MAPK-mediated signaling in the striatum/nucleus accumbens, registered them in KANPHOS, and analyzed the related pathways. |
format | Online Article Text |
id | pubmed-8750479 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-87504792022-01-12 KANPHOS: A Database of Kinase-Associated Neural Protein Phosphorylation in the Brain Ahammad, Rijwan Uddin Nishioka, Tomoki Yoshimoto, Junichiro Kannon, Takayuki Amano, Mutsuki Funahashi, Yasuhiro Tsuboi, Daisuke Faruk, Md. Omar Yamahashi, Yukie Yamada, Kiyofumi Nagai, Taku Kaibuchi, Kozo Cells Article Protein phosphorylation plays critical roles in a variety of intracellular signaling pathways and physiological functions that are controlled by neurotransmitters and neuromodulators in the brain. Dysregulation of these signaling pathways has been implicated in neurodevelopmental disorders, including autism spectrum disorder, attention deficit hyperactivity disorder and schizophrenia. While recent advances in mass spectrometry-based proteomics have allowed us to identify approximately 280,000 phosphorylation sites, it remains largely unknown which sites are phosphorylated by which kinases. To overcome this issue, previously, we developed methods for comprehensive screening of the target substrates of given kinases, such as PKA and Rho-kinase, upon stimulation by extracellular signals and identified many candidate substrates for specific kinases and their phosphorylation sites. Here, we developed a novel online database to provide information about the phosphorylation signals identified by our methods, as well as those previously reported in the literature. The “KANPHOS” (Kinase-Associated Neural Phospho-Signaling) database and its web portal were built based on a next-generation XooNIps neuroinformatics tool. To explore the functionality of the KANPHOS database, we obtained phosphoproteomics data for adenosine-A2A-receptor signaling and its downstream MAPK-mediated signaling in the striatum/nucleus accumbens, registered them in KANPHOS, and analyzed the related pathways. MDPI 2021-12-24 /pmc/articles/PMC8750479/ /pubmed/35011609 http://dx.doi.org/10.3390/cells11010047 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Ahammad, Rijwan Uddin Nishioka, Tomoki Yoshimoto, Junichiro Kannon, Takayuki Amano, Mutsuki Funahashi, Yasuhiro Tsuboi, Daisuke Faruk, Md. Omar Yamahashi, Yukie Yamada, Kiyofumi Nagai, Taku Kaibuchi, Kozo KANPHOS: A Database of Kinase-Associated Neural Protein Phosphorylation in the Brain |
title | KANPHOS: A Database of Kinase-Associated Neural Protein Phosphorylation in the Brain |
title_full | KANPHOS: A Database of Kinase-Associated Neural Protein Phosphorylation in the Brain |
title_fullStr | KANPHOS: A Database of Kinase-Associated Neural Protein Phosphorylation in the Brain |
title_full_unstemmed | KANPHOS: A Database of Kinase-Associated Neural Protein Phosphorylation in the Brain |
title_short | KANPHOS: A Database of Kinase-Associated Neural Protein Phosphorylation in the Brain |
title_sort | kanphos: a database of kinase-associated neural protein phosphorylation in the brain |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8750479/ https://www.ncbi.nlm.nih.gov/pubmed/35011609 http://dx.doi.org/10.3390/cells11010047 |
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