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Article: Ser

Shao, Jieya

Molecular & cellular oncology

2020 Volume 7, Issue 5, Page(s) 1796179

Abstract: Valosin-containing protein (VCP) is essential for proteostasis during many cellular processes. However, it remains uncertain how its diverse functions are selectively regulated. We recently showed that DNA damage-induced ... ...

Abstract	Valosin-containing protein (VCP) is essential for proteostasis during many cellular processes. However, it remains uncertain how its diverse functions are selectively regulated. We recently showed that DNA damage-induced Ser
Language	English
Publishing date	2020-08-12
Publishing country	United States
Document type	Journal Article
ISSN	2372-3556
ISSN	2372-3556
DOI	10.1080/23723556.2020.1796179
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Article ; Online: Profilin-1 regulates DNA replication forks in a context-dependent fashion by interacting with SNF2H and BOD1L

Cuige Zhu / Mari Iwase / Ziqian Li / Faliang Wang / Annabel Quinet / Alessandro Vindigni / Jieya Shao

Nature Communications, Vol 13, Iss 1, Pp 1-

2022 Volume 19

Abstract: Subcellular localization plays an important yet underappreciated role in protein functions. Here the authors defined novel and context-dependent nuclear functions of the actin-binding factor profilin-1 in DNA replication fork dynamics and stability. ...

Abstract	Subcellular localization plays an important yet underappreciated role in protein functions. Here the authors defined novel and context-dependent nuclear functions of the actin-binding factor profilin-1 in DNA replication fork dynamics and stability.
Keywords	Science ; Q
Language	English
Publishing date	2022-11-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Profilin-1 regulates DNA replication forks in a context-dependent fashion by interacting with SNF2H and BOD1L.

Zhu, Cuige / Iwase, Mari / Li, Ziqian / Wang, Faliang / Quinet, Annabel / Vindigni, Alessandro / Shao, Jieya

Nature communications

2022 Volume 13, Issue 1, Page(s) 6531

Abstract: DNA replication forks are tightly controlled by a large protein network consisting of well-known core regulators and many accessory factors which remain functionally undefined. In this study, we report previously unknown nuclear functions of the actin- ... ...

Abstract	DNA replication forks are tightly controlled by a large protein network consisting of well-known core regulators and many accessory factors which remain functionally undefined. In this study, we report previously unknown nuclear functions of the actin-binding factor profilin-1 (PFN1) in DNA replication, which occur in a context-dependent fashion and require its binding to poly-L-proline (PLP)-containing proteins instead of actin. In unperturbed cells, PFN1 increases DNA replication initiation and accelerates fork progression by binding and stimulating the PLP-containing nucleosome remodeler SNF2H. Under replication stress, PFN1/SNF2H increases fork stalling and functionally collaborates with fork reversal enzymes to enable the over-resection of unprotected forks. In addition, PFN1 binds and functionally attenuates the PLP-containing fork protector BODL1 to increase the resection of a subset of stressed forks. Accordingly, raising nuclear PFN1 level decreases genome stability and cell survival during replication stress. Thus, PFN1 is a multi-functional regulator of DNA replication with exploitable anticancer potential.
MeSH term(s)	Humans ; Actins/metabolism ; DNA Helicases/metabolism ; DNA Replication ; Genomic Instability ; Profilins/metabolism ; Adenosine Triphosphatases/metabolism ; Chromosomal Proteins, Non-Histone/metabolism
Chemical Substances	Actins ; DNA Helicases (EC 3.6.4.-) ; PFN1 protein, human ; Profilins ; Adenosine Triphosphatases (EC 3.6.1.-) ; Chromosomal Proteins, Non-Histone
Language	English
Publishing date	2022-11-01
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-022-34310-9
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Article: Phospho-Ser

Wang, Faliang / Vij, Kiran / Li, Lin / Dodhiawala, Paarth / Lim, Kian-Huat / Shao, Jieya

Cancers

2021 Volume 13, Issue 20

Abstract: Pancreatic ductal adenocarcinoma (PDAC) patients have a dismal prognosis due in large part to chemotherapy resistance. However, a small subset containing defects in the DNA damage response (DDR) pathways are chemotherapy-sensitive. Identifying intrinsic ... ...

Abstract	Pancreatic ductal adenocarcinoma (PDAC) patients have a dismal prognosis due in large part to chemotherapy resistance. However, a small subset containing defects in the DNA damage response (DDR) pathways are chemotherapy-sensitive. Identifying intrinsic and therapeutically inducible DDR defects can improve precision and efficacy of chemotherapies for PDAC. DNA repair requires dynamic reorganization of chromatin-associated proteins, which is orchestrated by the AAA+ ATPase VCP. We recently discovered that the DDR function of VCP is selectively activated by Ser
Language	English
Publishing date	2021-10-11
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2527080-1
ISSN	2072-6694
ISSN	2072-6694
DOI	10.3390/cancers13205076
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Article: Ser

Wang, Faliang / Zhu, Cuige / Cai, Shirong / Boudreau, Aaron / Kim, Sun-Joong / Bissell, Mina / Shao, Jieya

Frontiers in cell and developmental biology

2021 Volume 9, Page(s) 692269

Abstract: The essential actin-binding factor profilin-1 (Pfn1) is a non-classical tumor suppressor with the abilities toboth inhibit cellular proliferation and augment chemotherapy-induced apoptosis. Besides actin, Pfn1 interacts with proteins harboring the poly-L- ...

Abstract	The essential actin-binding factor profilin-1 (Pfn1) is a non-classical tumor suppressor with the abilities toboth inhibit cellular proliferation and augment chemotherapy-induced apoptosis. Besides actin, Pfn1 interacts with proteins harboring the poly-L-proline (PLP) motifs. Our recent work demonstrated that both nuclear localization and PLP-binding are required for tumor growth inhibition by Pfn1, and this is at least partially due to Pfn1 association with the PLP-containing ENL protein in the Super Elongation Complex (SEC) and the transcriptional inhibition of pro-cancer genes. In this paper, by identifying a phosphorylation event of Pfn1 at Ser
Language	English
Publishing date	2021-06-21
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2021.692269
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Article ; Online: Ser71 Phosphorylation Inhibits Actin-Binding of Profilin-1 and Its Apoptosis-Sensitizing Activity

Faliang Wang / Cuige Zhu / Shirong Cai / Aaron Boudreau / Sun-Joong Kim / Mina Bissell / Jieya Shao

Frontiers in Cell and Developmental Biology, Vol

2021 Volume 9

Abstract	The essential actin-binding factor profilin-1 (Pfn1) is a non-classical tumor suppressor with the abilities toboth inhibit cellular proliferation and augment chemotherapy-induced apoptosis. Besides actin, Pfn1 interacts with proteins harboring the poly-L-proline (PLP) motifs. Our recent work demonstrated that both nuclear localization and PLP-binding are required for tumor growth inhibition by Pfn1, and this is at least partially due to Pfn1 association with the PLP-containing ENL protein in the Super Elongation Complex (SEC) and the transcriptional inhibition of pro-cancer genes. In this paper, by identifying a phosphorylation event of Pfn1 at Ser71 capable of inhibiting its actin-binding and nuclear export, we provide in vitro and in vivo evidence that chemotherapy-induced apoptotic sensitization by Pfn1 requires its cytoplasmic localization and actin-binding. With regard to tumor growth inhibition byPfn1, our data indicate a requirement for dynamic actin association and dissociation rendered by reversible Ser71phosphorylation and dephosphorylation. Furthermore, genetic and pharmacological experiments showed that Ser71 of Pfn1 can be phosphorylated by protein kinase A (PKA). Taken together, our data provide novel mechanistic insights into the multifaceted anticancer activities of Pfn1 and how they are spatially-defined in the cell and differentially regulated by ligand-binding.
Keywords	profilin-1 ; phosphorylation ; actin ; poly-L-proline ; apoptosis ; breast cancer ; Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2021-06-01T00:00:00Z
Publisher	Frontiers Media S.A.
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Gamma synuclein promotes cancer metastasis through the MKK3/6-p38MAPK cascade.

Liu, Jieya / Shao, Ting / Zhang, Jin / Liu, Qianyi / Hua, Hui / Zhang, Hongying / Wang, Jiao / Luo, Ting / Shi, Yuenian Eric / Jiang, Yangfu

International journal of biological sciences

2022 Volume 18, Issue 8, Page(s) 3167–3177

Abstract: Gamma synuclein (SNCG) is a neuronal protein that is also aberrantly overexpressed in various types of human cancer. SNCG overexpression promotes cancer invasion and metastasis. However, the mechanisms that drive cancer metastasis upon SNCG expression ... ...

Abstract	Gamma synuclein (SNCG) is a neuronal protein that is also aberrantly overexpressed in various types of human cancer. SNCG overexpression promotes cancer invasion and metastasis. However, the mechanisms that drive cancer metastasis upon SNCG expression remain elusive. Elucidation of the mechanisms underlying the promotion of cancer metastasis by SNCG may help discover therapeutic avenues for SNCG-overexpressed cancer. Here, we show that SNCG promotes transforming growth factor-β (TGF-β)-induced p38 mitogen-activated protein kinase (MAPK) phosphorylation. Mechanistically, SNCG promotes p38MAPK phosphorylation by interacting with the MAPK kinase 3/6 (MKK3/6) and prevents their degradation. SNCG knockdown leads to a decrease in TGF-β-induced phosphorylation of MKK3/6; and abrogates the induction of matrix metalloproteinase (MMP)-9 expression by TGF-β and its target gene Twist1. Furthermore, p38MAPK inhibition abrogates the promotion of MMP-9 expression and cancer cell invasion by SNCG. Both p38MAPK and MMP inhibitors can suppress the promotion of cancer cell invasion by SNCG. Finally, overexpression of SNCG in liver cancer cells promotes lung metastasis, which can be suppressed by the p38MAPK inhibitor. Together, our data uncover a previously unknown role of SNCG in promoting TGF-β-MKK3/6-p38MAPK signaling. This study highlights the critical role of p38MAPK in the promotion of cancer metastasis by SNCG, and indicates that p38MAPK inhibitor may serve as a potential therapeutic for SNCG-overexpressed cancer.
MeSH term(s)	Humans ; MAP Kinase Kinase 3 ; MAP Kinase Kinase 6 ; MAP Kinase Signaling System/genetics ; Neoplasm Invasiveness ; Neoplasm Metastasis ; Neoplasm Proteins ; Transforming Growth Factor beta/metabolism ; gamma-Synuclein/genetics ; gamma-Synuclein/metabolism ; p38 Mitogen-Activated Protein Kinases/metabolism
Chemical Substances	Neoplasm Proteins ; SNCG protein, human ; Transforming Growth Factor beta ; gamma-Synuclein ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; MAP Kinase Kinase 3 (EC 2.7.12.2) ; MAP Kinase Kinase 6 (EC 2.7.12.2) ; MAP2K3 protein, human (EC 2.7.12.2) ; MAP2K6 protein, human (EC 2.7.12.2)
Language	English
Publishing date	2022-05-01
Publishing country	Australia
Document type	Journal Article
ZDB-ID	2179208-2
ISSN	1449-2288 ; 1449-2288
ISSN (online)	1449-2288
ISSN	1449-2288
DOI	10.7150/ijbs.69155
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Article ; Online: Protein phosphatase 1 dephosphorylates profilin-1 at Ser-137.

Jieya Shao / Marc I Diamond

PLoS ONE, Vol 7, Iss 3, p e

2012 Volume 32802

Abstract: Profilin-1 (PFN1) plays an important role in the control of actin dynamics, and could represent an important therapeutic target in several diseases. We previously identified PFN1 as a huntingtin aggregation inhibitor, and others have implicated it as a ... ...

Abstract	Profilin-1 (PFN1) plays an important role in the control of actin dynamics, and could represent an important therapeutic target in several diseases. We previously identified PFN1 as a huntingtin aggregation inhibitor, and others have implicated it as a tumor-suppressor. Rho-associated kinase (ROCK) directly phosphorylates PFN1 at Ser-137 to prevent its binding to polyproline sequences. This negatively regulates its anti-aggregation activity. However, the phosphatase that dephosphorylates PFN1 at Ser-137, and thus activates it, is unknown. Using a phospho-specific antibody against Ser-137 of PFN1, we characterized PFN1 dephosphorylation in cultured cells based on immunocytochemistry and a quantitative plate reader-based assay. Both okadaic acid and endothall increased pS137-PFN1 levels at concentrations more consistent with their known IC(50)s for protein phosphatase 1 (PP1) than protein phosphatase 2A (PP2A). Knockdown of the catalytic subunit of PP1 (PP1Cα), but not PP2A (PP2ACα), increased pS137-PFN1 levels. PP1Cα binds PFN1 in cultured cells, and this interaction was increased by a phosphomimetic mutation of PFN1 at Ser-137 (S137D). Together, these data define PP1 as the principal phosphatase for Ser-137 of PFN1, and provide mechanistic insights into PFN1 regulation by phosphorylation.
Keywords	Medicine ; R ; Science ; Q
Language	English
Publishing date	2012-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Protein phosphatase 1 dephosphorylates profilin-1 at Ser-137.

Shao, Jieya / Diamond, Marc I

PloS one

2012 Volume 7, Issue 3, Page(s) e32802

Abstract	Profilin-1 (PFN1) plays an important role in the control of actin dynamics, and could represent an important therapeutic target in several diseases. We previously identified PFN1 as a huntingtin aggregation inhibitor, and others have implicated it as a tumor-suppressor. Rho-associated kinase (ROCK) directly phosphorylates PFN1 at Ser-137 to prevent its binding to polyproline sequences. This negatively regulates its anti-aggregation activity. However, the phosphatase that dephosphorylates PFN1 at Ser-137, and thus activates it, is unknown. Using a phospho-specific antibody against Ser-137 of PFN1, we characterized PFN1 dephosphorylation in cultured cells based on immunocytochemistry and a quantitative plate reader-based assay. Both okadaic acid and endothall increased pS137-PFN1 levels at concentrations more consistent with their known IC(50)s for protein phosphatase 1 (PP1) than protein phosphatase 2A (PP2A). Knockdown of the catalytic subunit of PP1 (PP1Cα), but not PP2A (PP2ACα), increased pS137-PFN1 levels. PP1Cα binds PFN1 in cultured cells, and this interaction was increased by a phosphomimetic mutation of PFN1 at Ser-137 (S137D). Together, these data define PP1 as the principal phosphatase for Ser-137 of PFN1, and provide mechanistic insights into PFN1 regulation by phosphorylation.
MeSH term(s)	Animals ; Blotting, Western ; Dicarboxylic Acids/pharmacology ; Dose-Response Relationship, Drug ; HEK293 Cells ; HeLa Cells ; Humans ; Immunohistochemistry ; Mice ; NIH 3T3 Cells ; Okadaic Acid/pharmacology ; Phosphorylation/drug effects ; Profilins/genetics ; Profilins/metabolism ; Protein Binding ; Protein Phosphatase 1/antagonists & inhibitors ; Protein Phosphatase 1/genetics ; Protein Phosphatase 1/metabolism ; Protein Phosphatase 2/antagonists & inhibitors ; Protein Phosphatase 2/genetics ; Protein Phosphatase 2/metabolism ; RNA Interference ; Serine/genetics ; Serine/metabolism
Chemical Substances	Dicarboxylic Acids ; PFN1 protein, human ; Profilins ; endothall (145-73-3) ; Okadaic Acid (1W21G5Q4N2) ; Serine (452VLY9402) ; Protein Phosphatase 1 (EC 3.1.3.16) ; Protein Phosphatase 2 (EC 3.1.3.16)
Language	English
Publishing date	2012-03-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0032802
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Article ; Online: Cancer-associated exportin-6 upregulation inhibits the transcriptionally repressive and anticancer effects of nuclear profilin-1.

Zhu, Cuige / Kim, Sun-Joong / Mooradian, Arshag / Wang, Faliang / Li, Ziqian / Holohan, Sean / Collins, Patrick L / Wang, Keren / Guo, Zhanfang / Hoog, Jeremy / Ma, Cynthia X / Oltz, Eugene M / Held, Jason M / Shao, Jieya

Cell reports

2021 Volume 34, Issue 7, Page(s) 108749

Abstract: Aberrant expression of nuclear transporters and deregulated subcellular localization of their cargo proteins are emerging as drivers and therapeutic targets of cancer. Here, we present evidence that the nuclear exporter exportin-6 and its cargo profilin- ... ...

Abstract	Aberrant expression of nuclear transporters and deregulated subcellular localization of their cargo proteins are emerging as drivers and therapeutic targets of cancer. Here, we present evidence that the nuclear exporter exportin-6 and its cargo profilin-1 constitute a functionally important and frequently deregulated axis in cancer. Exportin-6 upregulation occurs in numerous cancer types and is associated with poor patient survival. Reducing exportin-6 level in breast cancer cells triggers antitumor effects by accumulating nuclear profilin-1. Mechanistically, nuclear profilin-1 interacts with eleven-nineteen-leukemia protein (ENL) within the super elongation complex (SEC) and inhibits the ability of the SEC to drive transcription of numerous pro-cancer genes including MYC. XPO6 and MYC are positively correlated across diverse cancer types including breast cancer. Therapeutically, exportin-6 loss sensitizes breast cancer cells to the bromodomain and extra-terminal (BET) inhibitor JQ1. Thus, exportin-6 upregulation is a previously unrecognized cancer driver event by spatially inhibiting nuclear profilin-1 as a tumor suppressor.
MeSH term(s)	Animals ; Cell Line, Tumor ; Female ; Heterografts ; Humans ; Karyopherins/genetics ; Karyopherins/metabolism ; MCF-7 Cells ; Mice ; Mice, Nude ; Neoplasms/genetics ; Neoplasms/metabolism ; Profilins/antagonists & inhibitors ; Profilins/genetics ; Profilins/metabolism ; Survival Analysis ; Up-Regulation
Chemical Substances	Karyopherins ; PFN1 protein, human ; Profilins ; XPO6 protein, human
Language	English
Publishing date	2021-02-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2021.108749
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