LIVIVO - Search results -

Search results

Result 1 - 10 of total 83

Article ; Online: Xenopus

Liu, Junjun / Zhang, Chuanmao

Biophysics reports

2022 Volume 9, Issue 4, Page(s) 195–205

Abstract: ... ...

Abstract	Xenopus
Language	English
Publishing date	2022-07-18
Publishing country	China
Document type	Journal Article
ISSN	2364-3420
ISSN (online)	2364-3420
DOI	10.52601/bpr.2023.230016
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Live-cell fluorescence imaging of ciliary dynamics.

Lü, Quanlong / Zhang, Chuanmao / Westlake, Christopher J

Biophysics reports

2023 Volume 7, Issue 2, Page(s) 101–110

Abstract: The cilium was one of the first organelles observed through a microscope. Motile cilia appear as oscillating cell appendages and have long been recognized to function in cell motility. In contrast, the far more widespread non-motile cilia, termed primary ...

Abstract	The cilium was one of the first organelles observed through a microscope. Motile cilia appear as oscillating cell appendages and have long been recognized to function in cell motility. In contrast, the far more widespread non-motile cilia, termed primary cilia, were thought to be vestigial and largely ignored following their initial description over a century ago. Only in the last two decades has the critical function of primary cilia been elucidated. Primary cilia play essential roles in signal transduction, chemical sensation, mechanosensation and light detection. Various microscopy approaches have been important for characterizing the structure, dynamics and function of the cilia. In this review, we discuss the application of live-cell imaging technologies and their contribution to our current understanding of ciliary processes.
Language	English
Publishing date	2023-05-23
Publishing country	China
Document type	Journal Article
ISSN	2364-3420
ISSN (online)	2364-3420
DOI	10.52601/bpr.2021.210005
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: NuSAP regulates microtubule flux and Kif2A localization to ensure accurate chromosome congression.

Sun, Mengjie / Wang, Yao / Xin, Guangwei / Yang, Biying / Jiang, Qing / Zhang, Chuanmao

The Journal of cell biology

2023 Volume 223, Issue 2

Abstract: Precise chromosome congression and segregation requires the proper assembly of a steady-state metaphase spindle, which is dynamic and maintained by continuous microtubule flux. NuSAP is a microtubule-stabilizing and -bundling protein that promotes ... ...

Abstract	Precise chromosome congression and segregation requires the proper assembly of a steady-state metaphase spindle, which is dynamic and maintained by continuous microtubule flux. NuSAP is a microtubule-stabilizing and -bundling protein that promotes chromosome-dependent spindle assembly. However, its function in spindle dynamics remains unclear. Here, we demonstrate that NuSAP regulates the metaphase spindle length control. Mechanistically, NuSAP facilitates kinetochore capture and spindle assembly by promoting Eg5 binding to microtubules. It also prevents excessive microtubule depolymerization through interaction with Kif2A, which reduces Kif2A spindle-pole localization. NuSAP is phosphorylated by Aurora A at Ser-240 during mitosis, and this phosphorylation promotes its interaction with Kif2A on the spindle body and reduces its localization with the spindle poles, thus maintaining proper spindle microtubule flux. NuSAP knockout resulted in the formation of shorter spindles with faster microtubule flux and chromosome misalignment. Taken together, we uncover that NuSAP participates in spindle assembly, dynamics, and metaphase spindle length control through the regulation of microtubule flux and Kif2A localization.
MeSH term(s)	Humans ; Chromosome Segregation ; HeLa Cells ; Kinesins/genetics ; Kinesins/metabolism ; Kinetochores/metabolism ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Microtubules/genetics ; Microtubules/metabolism ; Mitosis ; Spindle Apparatus/genetics ; Spindle Apparatus/metabolism
Chemical Substances	Kinesins (EC 3.6.4.4) ; Microtubule-Associated Proteins ; KIF2A protein, human ; NUSAP1 protein, human
Language	English
Publishing date	2023-12-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202108070
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ub I Zs.190: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: 8 Å structure of the outer rings of the Xenopus laevis nuclear pore complex obtained by cryo-EM and AI.

Tai, Linhua / Zhu, Yun / Ren, He / Huang, Xiaojun / Zhang, Chuanmao / Sun, Fei

Protein & cell

2022 Volume 13, Issue 10, Page(s) 760–777

Abstract: The nuclear pore complex (NPC), one of the largest protein complexes in eukaryotes, serves as a physical gate to regulate nucleocytoplasmic transport. Here, we determined the 8 Å resolution cryo-electron microscopic (cryo-EM) structure of the outer rings ...

Abstract	The nuclear pore complex (NPC), one of the largest protein complexes in eukaryotes, serves as a physical gate to regulate nucleocytoplasmic transport. Here, we determined the 8 Å resolution cryo-electron microscopic (cryo-EM) structure of the outer rings containing nuclear ring (NR) and cytoplasmic ring (CR) from the Xenopus laevis NPC, with local resolutions reaching 4.9 Å. With the aid of AlphaFold2, we managed to build a pseudoatomic model of the outer rings, including the Y complexes and flanking components. In this most comprehensive and accurate model of outer rings to date, the almost complete Y complex structure exhibits much tighter interaction in the hub region. In addition to two copies of Y complexes, each asymmetric subunit in CR contains five copies of Nup358, two copies of the Nup214 complex, two copies of Nup205 and one copy of newly identified Nup93, while that in NR contains one copy of Nup205, one copy of ELYS and one copy of Nup93. These in-depth structural features represent a great advance in understanding the assembly of NPCs.
MeSH term(s)	Animals ; Artificial Intelligence ; Cryoelectron Microscopy ; Nuclear Pore/chemistry ; Nuclear Pore/metabolism ; Nuclear Pore/ultrastructure ; Oocytes/metabolism ; Xenopus laevis
Language	English
Publishing date	2022-01-11
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2543451-2
ISSN	1674-8018 ; 1674-800X
ISSN (online)	1674-8018
ISSN	1674-800X
DOI	10.1007/s13238-021-00895-y
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Cartwheel disassembly regulated by CDK1-Cyclin B kinase allows human centriole disengagement and licensing.

Huang, Fan / Xu, Xiaowei / Xin, Guangwei / Zhang, Boyan / Jiang, Qing / Zhang, Chuanmao

The Journal of biological chemistry

2022 , Page(s) 102658

Abstract: Cartwheel assembly is considered the first step in the initiation of procentriole biogenesis; however, the reason for persistence of the assembled human cartwheel structure from S phase to late mitosis remains unclear. Here, we demonstrate mainly using ... ...

Abstract	Cartwheel assembly is considered the first step in the initiation of procentriole biogenesis; however, the reason for persistence of the assembled human cartwheel structure from S phase to late mitosis remains unclear. Here, we demonstrate mainly using cell synchronization, RNA interference, immunofluorescence and time-lapse-microscopy, biochemical analysis and methods that the cartwheel persistently assembles and maintains centriole engagement and centrosome integrity during S phase to late G2 phase. Blockade of the continuous accumulation of centriolar Sas-6, a major cartwheel protein, after procentriole formation induces premature centriole disengagement and disrupts pericentriolar matrix integrity. Additionally, we determined that during mitosis, CDK1-Cyclin B phosphorylates Sas-6 at T495 and S510, disrupting its binding to cartwheel component STIL and pericentriolar component Nedd1 and promoting cartwheel disassembly and centriole disengagement. Perturbation of this phosphorylation maintains the accumulation of centriolar Sas-6 and retains centriole engagement during mitotic exit, which results in the inhibition of centriole reduplication. Collectively, these data demonstrate that persistent cartwheel assembly after procentriole formation maintains centriole engagement and that this configuration is relieved through phosphorylation of Sas-6 by CDK1-Cyclin B during mitosis in human cells.
Language	English
Publishing date	2022-11-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.102658
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: The equilibrium of ubiquitination and deubiquitination at PLK1 regulates sister chromatid separation.

Liu, Junjun / Zhang, Chuanmao

Cellular and molecular life sciences : CMLS

2017 Volume 74, Issue 12, Page(s) 2127–2134

Abstract: PLK1 regulates almost every aspect of mitotic events, including mitotic entry, spindle assembly, chromosome alignment, sister chromatid segregation, metaphase-anaphase transition, cytokinesis, etc. In regulating the chromosome alignment and sister ... ...

Abstract	PLK1 regulates almost every aspect of mitotic events, including mitotic entry, spindle assembly, chromosome alignment, sister chromatid segregation, metaphase-anaphase transition, cytokinesis, etc. In regulating the chromosome alignment and sister chromatid segregation, PLK1 has to be localized to and removed from kinetochores at the right times, and the underlying mechanism that regulates PLK1 both spatially and temporally only became clearer recently. It has been found that deubiquitination and ubiquitination of PLK1 are responsible for its localization to and dissociation from the kinetochores, respectively. The equilibrium of this ubiquitination and deubiquitination plays an important role in regulating proper chromosome alignment and timely sister chromatid segregation. Here, we summarize and discuss the recent findings in investigating the spatial and temporal regulation of PLK1 during chromosome alignment and sister chromatid segregation.
MeSH term(s)	Animals ; Cell Cycle ; Cell Cycle Proteins/metabolism ; Chromatids/metabolism ; Humans ; Kinetochores/metabolism ; Protein Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism ; Substrate Specificity ; Ubiquitination ; Polo-Like Kinase 1
Chemical Substances	Cell Cycle Proteins ; Proto-Oncogene Proteins ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2017-02-10
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-017-2457-5
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 195: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: PLK4-phosphorylated NEDD1 facilitates cartwheel assembly and centriole biogenesis initiations.

Chi, Wangfei / Wang, Gang / Xin, Guangwei / Jiang, Qing / Zhang, Chuanmao

The Journal of cell biology

2020 Volume 220, Issue 1

Abstract: Centrosome duplication occurs under strict spatiotemporal regulation once per cell cycle, and it begins with cartwheel assembly and daughter centriole biogenesis at the lateral sites of the mother centrioles. However, although much of this process is ... ...

Abstract	Centrosome duplication occurs under strict spatiotemporal regulation once per cell cycle, and it begins with cartwheel assembly and daughter centriole biogenesis at the lateral sites of the mother centrioles. However, although much of this process is understood, how centrosome duplication is initiated remains unclear. Here, we show that cartwheel assembly followed by daughter centriole biogenesis is initiated on the NEDD1-containing layer of the pericentriolar material (PCM) by the recruitment of SAS-6 to the mother centriole under the regulation of PLK4. We found that PLK4-mediated phosphorylation of NEDD1 at its S325 amino acid residue directly promotes both NEDD1 binding to SAS-6 and recruiting SAS-6 to the centrosome. Overexpression of phosphomimicking NEDD1 mutant S325E promoted cartwheel assembly and daughter centriole biogenesis initiations, whereas overexpression of nonphosphorylatable NEDD1 mutant S325A abolished the initiations. Collectively, our results demonstrate that PLK4-regulated NEDD1 facilitates initiation of the cartwheel assembly and of daughter centriole biogenesis in mammals.
MeSH term(s)	Amino Acid Sequence ; Cell Cycle Proteins/metabolism ; Cell Line, Tumor ; Centrioles/metabolism ; Centrosome/metabolism ; HEK293 Cells ; Humans ; Microtubule-Associated Proteins/metabolism ; Models, Biological ; Mutant Proteins/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Protein Binding ; Protein-Serine-Threonine Kinases/metabolism ; Tubulin/metabolism
Chemical Substances	Cell Cycle Proteins ; Microtubule-Associated Proteins ; Mutant Proteins ; NEDD1 protein, human ; SASS6 protein, human ; Tubulin ; Phosphoserine (17885-08-4) ; PLK4 protein, human (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2020-12-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.202002151
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ub I Zs.190: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Stay in touch with the endoplasmic reticulum.

Sun, Sha / Zhao, Gan / Jia, Mingkang / Jiang, Qing / Li, Shulin / Wang, Haibin / Li, Wenjing / Wang, Yunyun / Bian, Xin / Zhao, Yan G / Huang, Xun / Yang, Ge / Cai, Huaqing / Pastor-Pareja, Jose C / Ge, Liang / Zhang, Chuanmao / Hu, Junjie

Science China. Life sciences

2024 Volume 67, Issue 2, Page(s) 230–257

Abstract: The endoplasmic reticulum (ER), which is composed of a continuous network of tubules and sheets, forms the most widely distributed membrane system in eukaryotic cells. As a result, it engages a variety of organelles by establishing membrane contact sites ...

Abstract	The endoplasmic reticulum (ER), which is composed of a continuous network of tubules and sheets, forms the most widely distributed membrane system in eukaryotic cells. As a result, it engages a variety of organelles by establishing membrane contact sites (MCSs). These contacts regulate organelle positioning and remodeling, including fusion and fission, facilitate precise lipid exchange, and couple vital signaling events. Here, we systematically review recent advances and converging themes on ER-involved organellar contact. The molecular basis, cellular influence, and potential physiological functions for ER/nuclear envelope contacts with mitochondria, Golgi, endosomes, lysosomes, lipid droplets, autophagosomes, and plasma membrane are summarized.
MeSH term(s)	Endoplasmic Reticulum/metabolism ; Golgi Apparatus/metabolism ; Cell Membrane/metabolism ; Mitochondria/metabolism ; Lysosomes/metabolism ; Endosomes/metabolism
Language	English
Publishing date	2024-01-04
Publishing country	China
Document type	Systematic Review ; Journal Article ; Review
ZDB-ID	2546732-3
ISSN	1869-1889 ; 1674-7305
ISSN (online)	1869-1889
ISSN	1674-7305
DOI	10.1007/s11427-023-2443-9
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: Aurora B regulates PP1γ-Repo-Man interactions to maintain the chromosome condensation state.

Xin, Guangwei / Fu, Jingyan / Luo, Jia / Deng, Zhaoxuan / Jiang, Qing / Zhang, Chuanmao

The Journal of biological chemistry

2020 Volume 295, Issue 43, Page(s) 14780–14788

Abstract: The mitotic kinase Aurora B regulates the condensation of chromatin into chromosomes by phosphorylating chromatin proteins during early mitosis, whereas the phosphatase PP1γ performs the opposite function. The roles of Aurora B and PP1γ must be tightly ... ...

Abstract	The mitotic kinase Aurora B regulates the condensation of chromatin into chromosomes by phosphorylating chromatin proteins during early mitosis, whereas the phosphatase PP1γ performs the opposite function. The roles of Aurora B and PP1γ must be tightly coordinated to maintain chromosomes at a high phosphorylation state, but the precise mechanisms regulating their function remain largely unclear. Here, mainly through immunofluorescence microscopy and co-immunoprecipitation assays, we find that dissociation of PP1γ from chromosomes is essential for maintaining chromosome phosphorylation. We uncover that PP1γ is recruited to mitotic chromosomes by its regulatory subunit Repo-Man in the absence of Aurora B activity and that Aurora B regulates dissociation of PP1γ by phosphorylating and disrupting PP1γ-Repo-Man interactions on chromatin. Overexpression of Repo-Man mutants that cannot be phosphorylated or inhibition of Aurora B kinase activity resulted in the retention of PP1γ on chromatin and prolonged the chromatin condensation process; a similar outcome was caused by the ectopic targeting of PP1γ to chromatin. Together, our findings reveal a novel regulation mechanism of chromatin condensation in which Aurora B counteracts PP1γ activity by releasing PP1γ from Repo-Man and may have important implications for understanding the regulations of dynamic structural changes of the chromosomes in mitosis.
MeSH term(s)	Aurora Kinase B/metabolism ; Carrier Proteins/metabolism ; Cell Cycle Proteins/metabolism ; Chromatin/metabolism ; Chromosomes, Human/metabolism ; HeLa Cells ; Humans ; Mitosis ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein Interaction Maps ; Protein Phosphatase 1/metabolism
Chemical Substances	CDCA2 protein, human ; Carrier Proteins ; Cell Cycle Proteins ; Chromatin ; Nuclear Proteins ; Aurora Kinase B (EC 2.7.11.1) ; Protein Phosphatase 1 (EC 3.1.3.16)
Language	English
Publishing date	2020-09-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.AC120.012772
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: NuMA regulates mitotic spindle assembly, structural dynamics and function via phase separation.

Sun, Mengjie / Jia, Mingkang / Ren, He / Yang, Biying / Chi, Wangfei / Xin, Guangwei / Jiang, Qing / Zhang, Chuanmao

Nature communications

2021 Volume 12, Issue 1, Page(s) 7157

Abstract: A functional mitotic spindle is essential for accurate chromosome congression and segregation during cell proliferation; however, the underlying mechanisms of its assembly remain unclear. Here we show that NuMA regulates this assembly process via phase ... ...

Abstract	A functional mitotic spindle is essential for accurate chromosome congression and segregation during cell proliferation; however, the underlying mechanisms of its assembly remain unclear. Here we show that NuMA regulates this assembly process via phase separation regulated by Aurora A. NuMA undergoes liquid-liquid phase separation during mitotic entry and KifC1 facilitates NuMA condensates concentrating on spindle poles. Phase separation of NuMA is mediated by its C-terminus, whereas its dynein-dynactin binding motif also facilitates this process. Phase-separated NuMA droplets concentrate tubulins, bind microtubules, and enrich crucial regulators, including Kif2A, at the spindle poles, which then depolymerizes spindle microtubules and promotes poleward spindle microtubule flux for spindle assembly and structural dynamics. In this work, we show that NuMA orchestrates mitotic spindle assembly, structural dynamics and function via liquid-liquid phase separation regulated by Aurora A phosphorylation.
MeSH term(s)	Aurora Kinase A/genetics ; Aurora Kinase A/metabolism ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Dynactin Complex/genetics ; Dynactin Complex/metabolism ; Dyneins/genetics ; Dyneins/metabolism ; HeLa Cells ; Humans ; Kinesins/genetics ; Kinesins/metabolism ; Microtubules/genetics ; Microtubules/metabolism ; Spindle Apparatus/chemistry ; Spindle Apparatus/genetics ; Spindle Apparatus/metabolism ; Tubulin/genetics ; Tubulin/metabolism
Chemical Substances	Cell Cycle Proteins ; Dynactin Complex ; KIFC1 protein, human ; NUMA1 protein, human ; Tubulin ; AURKA protein, human (EC 2.7.11.1) ; Aurora Kinase A (EC 2.7.11.1) ; Dyneins (EC 3.6.4.2) ; Kinesins (EC 3.6.4.4)
Language	English
Publishing date	2021-12-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-27528-6
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

To top

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito