Ohne Titel

Phosphorylation is a posttranslational modification of proteins that regulates many cellular processes, such as communication between cells, cell proliferation, cell movements, and gene expression. Therefore, many studies have been conducted to determine the significance and function of phosphorylat...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Hisanaga, Shin-ichi [verfasserIn] Krishnankutty, Ambika [verfasserIn] Kimura, Taeko [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	Phos-tag Phosphorylation Tau p35 Cdk5 activator GSK3β Tauopathy

Übergeordnetes Werk:	Enthalten in: Journal of proteomics - New York, NY [u.a.] : Elsevier, 2008, 262
Übergeordnetes Werk:	volume:262

DOI / URN:	10.1016/j.jprot.2022.104591

Katalog-ID:	ELV007924216

Internformat


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520			\|a Phosphorylation is a posttranslational modification of proteins that regulates many cellular processes, such as communication between cells, cell proliferation, cell movements, and gene expression. Therefore, many studies have been conducted to determine the significance and function of phosphorylation. These studies involve the identification of phosphorylation site(s), kinases and phosphatases, and regulatory mechanisms. Recently, phosphorylation sites were identified using mass spectrometry and detected by immunoblotting with phosphorylation site-specific antibodies. However, the in vivo phosphorylation profile of the target protein is not easy to grasp, and the quantification of site-specific phosphorylation is challenging if the protein is phosphorylated at multiple sites. Phos-tag is a phospho-affinity SDS–PAGE approach in which phosphorylated proteins are separated depending on the number and sites of phosphorylation during electrophoresis, which overcomes the aforementioned problems. We applied this technique to perform an in vivo analysis of the phosphorylation of many proteins. In this article, we show our results for the phosphorylation of tau protein, p35 Cdk5 activator and GSK3β to reveal the utility and power of this technique in protein phosphorylation analyses in vivo.Significant: We show the in vivo phosphorylation of tau and two tau kinases analysed by using Phos-tag SDS-PAGE. Tau represents about 12 different phosphoisotypes when expressed in cultured cells. Tau is differently phosphorylated in patients with different tauopathy. Phosphorylation of p35 Cdk5 activator, which suppress the abnormal activation of Cdk5 by cleavage with calpain, is regulated developmentally. The Ser9 phosphorylation is not a proper marker of the GSK3β activity in vivo.
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650		4	\|a Phosphorylation
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700	1		\|a Krishnankutty, Ambika \|e verfasserin \|4 aut
700	1		\|a Kimura, Taeko \|e verfasserin \|4 aut
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Indexfelder

author_variant	s i h sih a k ak t k tk
matchkey_str	article:18767737:2022----::
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publishDate	2022
allfields	10.1016/j.jprot.2022.104591 doi (DE-627)ELV007924216 (ELSEVIER)S1874-3919(22)00115-4 DE-627 ger DE-627 rda eng 570 540 DE-600 Hisanaga, Shin-ichi verfasserin aut 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Phosphorylation is a posttranslational modification of proteins that regulates many cellular processes, such as communication between cells, cell proliferation, cell movements, and gene expression. Therefore, many studies have been conducted to determine the significance and function of phosphorylation. These studies involve the identification of phosphorylation site(s), kinases and phosphatases, and regulatory mechanisms. Recently, phosphorylation sites were identified using mass spectrometry and detected by immunoblotting with phosphorylation site-specific antibodies. However, the in vivo phosphorylation profile of the target protein is not easy to grasp, and the quantification of site-specific phosphorylation is challenging if the protein is phosphorylated at multiple sites. Phos-tag is a phospho-affinity SDS–PAGE approach in which phosphorylated proteins are separated depending on the number and sites of phosphorylation during electrophoresis, which overcomes the aforementioned problems. We applied this technique to perform an in vivo analysis of the phosphorylation of many proteins. In this article, we show our results for the phosphorylation of tau protein, p35 Cdk5 activator and GSK3β to reveal the utility and power of this technique in protein phosphorylation analyses in vivo.Significant: We show the in vivo phosphorylation of tau and two tau kinases analysed by using Phos-tag SDS-PAGE. Tau represents about 12 different phosphoisotypes when expressed in cultured cells. Tau is differently phosphorylated in patients with different tauopathy. Phosphorylation of p35 Cdk5 activator, which suppress the abnormal activation of Cdk5 by cleavage with calpain, is regulated developmentally. The Ser9 phosphorylation is not a proper marker of the GSK3β activity in vivo. Phos-tag Phosphorylation Tau p35 Cdk5 activator GSK3β Tauopathy Krishnankutty, Ambika verfasserin aut Kimura, Taeko verfasserin aut Enthalten in Journal of proteomics New York, NY [u.a.] : Elsevier, 2008 262 Online-Ressource (DE-627)555688941 (DE-600)2400835-7 (DE-576)281507716 1876-7737 nnns volume:262 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 AR 262
spelling	10.1016/j.jprot.2022.104591 doi (DE-627)ELV007924216 (ELSEVIER)S1874-3919(22)00115-4 DE-627 ger DE-627 rda eng 570 540 DE-600 Hisanaga, Shin-ichi verfasserin aut 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Phosphorylation is a posttranslational modification of proteins that regulates many cellular processes, such as communication between cells, cell proliferation, cell movements, and gene expression. Therefore, many studies have been conducted to determine the significance and function of phosphorylation. These studies involve the identification of phosphorylation site(s), kinases and phosphatases, and regulatory mechanisms. Recently, phosphorylation sites were identified using mass spectrometry and detected by immunoblotting with phosphorylation site-specific antibodies. However, the in vivo phosphorylation profile of the target protein is not easy to grasp, and the quantification of site-specific phosphorylation is challenging if the protein is phosphorylated at multiple sites. Phos-tag is a phospho-affinity SDS–PAGE approach in which phosphorylated proteins are separated depending on the number and sites of phosphorylation during electrophoresis, which overcomes the aforementioned problems. We applied this technique to perform an in vivo analysis of the phosphorylation of many proteins. In this article, we show our results for the phosphorylation of tau protein, p35 Cdk5 activator and GSK3β to reveal the utility and power of this technique in protein phosphorylation analyses in vivo.Significant: We show the in vivo phosphorylation of tau and two tau kinases analysed by using Phos-tag SDS-PAGE. Tau represents about 12 different phosphoisotypes when expressed in cultured cells. Tau is differently phosphorylated in patients with different tauopathy. Phosphorylation of p35 Cdk5 activator, which suppress the abnormal activation of Cdk5 by cleavage with calpain, is regulated developmentally. The Ser9 phosphorylation is not a proper marker of the GSK3β activity in vivo. Phos-tag Phosphorylation Tau p35 Cdk5 activator GSK3β Tauopathy Krishnankutty, Ambika verfasserin aut Kimura, Taeko verfasserin aut Enthalten in Journal of proteomics New York, NY [u.a.] : Elsevier, 2008 262 Online-Ressource (DE-627)555688941 (DE-600)2400835-7 (DE-576)281507716 1876-7737 nnns volume:262 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 AR 262
allfields_unstemmed	10.1016/j.jprot.2022.104591 doi (DE-627)ELV007924216 (ELSEVIER)S1874-3919(22)00115-4 DE-627 ger DE-627 rda eng 570 540 DE-600 Hisanaga, Shin-ichi verfasserin aut 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Phosphorylation is a posttranslational modification of proteins that regulates many cellular processes, such as communication between cells, cell proliferation, cell movements, and gene expression. Therefore, many studies have been conducted to determine the significance and function of phosphorylation. These studies involve the identification of phosphorylation site(s), kinases and phosphatases, and regulatory mechanisms. Recently, phosphorylation sites were identified using mass spectrometry and detected by immunoblotting with phosphorylation site-specific antibodies. However, the in vivo phosphorylation profile of the target protein is not easy to grasp, and the quantification of site-specific phosphorylation is challenging if the protein is phosphorylated at multiple sites. Phos-tag is a phospho-affinity SDS–PAGE approach in which phosphorylated proteins are separated depending on the number and sites of phosphorylation during electrophoresis, which overcomes the aforementioned problems. We applied this technique to perform an in vivo analysis of the phosphorylation of many proteins. In this article, we show our results for the phosphorylation of tau protein, p35 Cdk5 activator and GSK3β to reveal the utility and power of this technique in protein phosphorylation analyses in vivo.Significant: We show the in vivo phosphorylation of tau and two tau kinases analysed by using Phos-tag SDS-PAGE. Tau represents about 12 different phosphoisotypes when expressed in cultured cells. Tau is differently phosphorylated in patients with different tauopathy. Phosphorylation of p35 Cdk5 activator, which suppress the abnormal activation of Cdk5 by cleavage with calpain, is regulated developmentally. The Ser9 phosphorylation is not a proper marker of the GSK3β activity in vivo. Phos-tag Phosphorylation Tau p35 Cdk5 activator GSK3β Tauopathy Krishnankutty, Ambika verfasserin aut Kimura, Taeko verfasserin aut Enthalten in Journal of proteomics New York, NY [u.a.] : Elsevier, 2008 262 Online-Ressource (DE-627)555688941 (DE-600)2400835-7 (DE-576)281507716 1876-7737 nnns volume:262 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 AR 262
allfieldsGer	10.1016/j.jprot.2022.104591 doi (DE-627)ELV007924216 (ELSEVIER)S1874-3919(22)00115-4 DE-627 ger DE-627 rda eng 570 540 DE-600 Hisanaga, Shin-ichi verfasserin aut 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Phosphorylation is a posttranslational modification of proteins that regulates many cellular processes, such as communication between cells, cell proliferation, cell movements, and gene expression. Therefore, many studies have been conducted to determine the significance and function of phosphorylation. These studies involve the identification of phosphorylation site(s), kinases and phosphatases, and regulatory mechanisms. Recently, phosphorylation sites were identified using mass spectrometry and detected by immunoblotting with phosphorylation site-specific antibodies. However, the in vivo phosphorylation profile of the target protein is not easy to grasp, and the quantification of site-specific phosphorylation is challenging if the protein is phosphorylated at multiple sites. Phos-tag is a phospho-affinity SDS–PAGE approach in which phosphorylated proteins are separated depending on the number and sites of phosphorylation during electrophoresis, which overcomes the aforementioned problems. We applied this technique to perform an in vivo analysis of the phosphorylation of many proteins. In this article, we show our results for the phosphorylation of tau protein, p35 Cdk5 activator and GSK3β to reveal the utility and power of this technique in protein phosphorylation analyses in vivo.Significant: We show the in vivo phosphorylation of tau and two tau kinases analysed by using Phos-tag SDS-PAGE. Tau represents about 12 different phosphoisotypes when expressed in cultured cells. Tau is differently phosphorylated in patients with different tauopathy. Phosphorylation of p35 Cdk5 activator, which suppress the abnormal activation of Cdk5 by cleavage with calpain, is regulated developmentally. The Ser9 phosphorylation is not a proper marker of the GSK3β activity in vivo. Phos-tag Phosphorylation Tau p35 Cdk5 activator GSK3β Tauopathy Krishnankutty, Ambika verfasserin aut Kimura, Taeko verfasserin aut Enthalten in Journal of proteomics New York, NY [u.a.] : Elsevier, 2008 262 Online-Ressource (DE-627)555688941 (DE-600)2400835-7 (DE-576)281507716 1876-7737 nnns volume:262 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 AR 262
allfieldsSound	10.1016/j.jprot.2022.104591 doi (DE-627)ELV007924216 (ELSEVIER)S1874-3919(22)00115-4 DE-627 ger DE-627 rda eng 570 540 DE-600 Hisanaga, Shin-ichi verfasserin aut 2022 nicht spezifiziert zzz rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Phosphorylation is a posttranslational modification of proteins that regulates many cellular processes, such as communication between cells, cell proliferation, cell movements, and gene expression. Therefore, many studies have been conducted to determine the significance and function of phosphorylation. These studies involve the identification of phosphorylation site(s), kinases and phosphatases, and regulatory mechanisms. Recently, phosphorylation sites were identified using mass spectrometry and detected by immunoblotting with phosphorylation site-specific antibodies. However, the in vivo phosphorylation profile of the target protein is not easy to grasp, and the quantification of site-specific phosphorylation is challenging if the protein is phosphorylated at multiple sites. Phos-tag is a phospho-affinity SDS–PAGE approach in which phosphorylated proteins are separated depending on the number and sites of phosphorylation during electrophoresis, which overcomes the aforementioned problems. We applied this technique to perform an in vivo analysis of the phosphorylation of many proteins. In this article, we show our results for the phosphorylation of tau protein, p35 Cdk5 activator and GSK3β to reveal the utility and power of this technique in protein phosphorylation analyses in vivo.Significant: We show the in vivo phosphorylation of tau and two tau kinases analysed by using Phos-tag SDS-PAGE. Tau represents about 12 different phosphoisotypes when expressed in cultured cells. Tau is differently phosphorylated in patients with different tauopathy. Phosphorylation of p35 Cdk5 activator, which suppress the abnormal activation of Cdk5 by cleavage with calpain, is regulated developmentally. The Ser9 phosphorylation is not a proper marker of the GSK3β activity in vivo. Phos-tag Phosphorylation Tau p35 Cdk5 activator GSK3β Tauopathy Krishnankutty, Ambika verfasserin aut Kimura, Taeko verfasserin aut Enthalten in Journal of proteomics New York, NY [u.a.] : Elsevier, 2008 262 Online-Ressource (DE-627)555688941 (DE-600)2400835-7 (DE-576)281507716 1876-7737 nnns volume:262 GBV_USEFLAG_U SYSFLAG_U GBV_ELV SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_224 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4338 GBV_ILN_4393 AR 262
language	English
source	Enthalten in Journal of proteomics 262 volume:262
sourceStr	Enthalten in Journal of proteomics 262 volume:262
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Phos-tag Phosphorylation Tau p35 Cdk5 activator GSK3β Tauopathy
dewey-raw	570
isfreeaccess_bool	false
container_title	Journal of proteomics
authorswithroles_txt_mv	Hisanaga, Shin-ichi @@aut@@ Krishnankutty, Ambika @@aut@@ Kimura, Taeko @@aut@@
publishDateDaySort_date	2022-01-01T00:00:00Z
hierarchy_top_id	555688941
dewey-sort	3570
id	ELV007924216
language_de	englisch
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author	Hisanaga, Shin-ichi
spellingShingle	Hisanaga, Shin-ichi ddc 570 misc Phos-tag misc Phosphorylation misc Tau misc p35 Cdk5 activator misc GSK3β misc Tauopathy
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topic_title	570 540 DE-600 Phos-tag Phosphorylation Tau p35 Cdk5 activator GSK3β Tauopathy
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abstract	Phosphorylation is a posttranslational modification of proteins that regulates many cellular processes, such as communication between cells, cell proliferation, cell movements, and gene expression. Therefore, many studies have been conducted to determine the significance and function of phosphorylation. These studies involve the identification of phosphorylation site(s), kinases and phosphatases, and regulatory mechanisms. Recently, phosphorylation sites were identified using mass spectrometry and detected by immunoblotting with phosphorylation site-specific antibodies. However, the in vivo phosphorylation profile of the target protein is not easy to grasp, and the quantification of site-specific phosphorylation is challenging if the protein is phosphorylated at multiple sites. Phos-tag is a phospho-affinity SDS–PAGE approach in which phosphorylated proteins are separated depending on the number and sites of phosphorylation during electrophoresis, which overcomes the aforementioned problems. We applied this technique to perform an in vivo analysis of the phosphorylation of many proteins. In this article, we show our results for the phosphorylation of tau protein, p35 Cdk5 activator and GSK3β to reveal the utility and power of this technique in protein phosphorylation analyses in vivo.Significant: We show the in vivo phosphorylation of tau and two tau kinases analysed by using Phos-tag SDS-PAGE. Tau represents about 12 different phosphoisotypes when expressed in cultured cells. Tau is differently phosphorylated in patients with different tauopathy. Phosphorylation of p35 Cdk5 activator, which suppress the abnormal activation of Cdk5 by cleavage with calpain, is regulated developmentally. The Ser9 phosphorylation is not a proper marker of the GSK3β activity in vivo.
abstractGer	Phosphorylation is a posttranslational modification of proteins that regulates many cellular processes, such as communication between cells, cell proliferation, cell movements, and gene expression. Therefore, many studies have been conducted to determine the significance and function of phosphorylation. These studies involve the identification of phosphorylation site(s), kinases and phosphatases, and regulatory mechanisms. Recently, phosphorylation sites were identified using mass spectrometry and detected by immunoblotting with phosphorylation site-specific antibodies. However, the in vivo phosphorylation profile of the target protein is not easy to grasp, and the quantification of site-specific phosphorylation is challenging if the protein is phosphorylated at multiple sites. Phos-tag is a phospho-affinity SDS–PAGE approach in which phosphorylated proteins are separated depending on the number and sites of phosphorylation during electrophoresis, which overcomes the aforementioned problems. We applied this technique to perform an in vivo analysis of the phosphorylation of many proteins. In this article, we show our results for the phosphorylation of tau protein, p35 Cdk5 activator and GSK3β to reveal the utility and power of this technique in protein phosphorylation analyses in vivo.Significant: We show the in vivo phosphorylation of tau and two tau kinases analysed by using Phos-tag SDS-PAGE. Tau represents about 12 different phosphoisotypes when expressed in cultured cells. Tau is differently phosphorylated in patients with different tauopathy. Phosphorylation of p35 Cdk5 activator, which suppress the abnormal activation of Cdk5 by cleavage with calpain, is regulated developmentally. The Ser9 phosphorylation is not a proper marker of the GSK3β activity in vivo.
abstract_unstemmed	Phosphorylation is a posttranslational modification of proteins that regulates many cellular processes, such as communication between cells, cell proliferation, cell movements, and gene expression. Therefore, many studies have been conducted to determine the significance and function of phosphorylation. These studies involve the identification of phosphorylation site(s), kinases and phosphatases, and regulatory mechanisms. Recently, phosphorylation sites were identified using mass spectrometry and detected by immunoblotting with phosphorylation site-specific antibodies. However, the in vivo phosphorylation profile of the target protein is not easy to grasp, and the quantification of site-specific phosphorylation is challenging if the protein is phosphorylated at multiple sites. Phos-tag is a phospho-affinity SDS–PAGE approach in which phosphorylated proteins are separated depending on the number and sites of phosphorylation during electrophoresis, which overcomes the aforementioned problems. We applied this technique to perform an in vivo analysis of the phosphorylation of many proteins. In this article, we show our results for the phosphorylation of tau protein, p35 Cdk5 activator and GSK3β to reveal the utility and power of this technique in protein phosphorylation analyses in vivo.Significant: We show the in vivo phosphorylation of tau and two tau kinases analysed by using Phos-tag SDS-PAGE. Tau represents about 12 different phosphoisotypes when expressed in cultured cells. Tau is differently phosphorylated in patients with different tauopathy. Phosphorylation of p35 Cdk5 activator, which suppress the abnormal activation of Cdk5 by cleavage with calpain, is regulated developmentally. The Ser9 phosphorylation is not a proper marker of the GSK3β activity in vivo.
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up_date	2024-07-06T17:56:17.848Z
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score	7.3985004

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