LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 9 of total 9

Search options

  1. Article ; Online: Cryo-EM structures of human magnesium channel MRS2 reveal gating and regulatory mechanisms.

    Lai, Louis Tung Faat / Balaraman, Jayashree / Zhou, Fei / Matthies, Doreen

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 7207

    Abstract: Magnesium ions ( ... ...

    Abstract Magnesium ions (Mg
    MeSH term(s) Humans ; Agaricales ; Cryoelectron Microscopy ; Magnesium ; Mitochondria ; Mitochondrial Membranes ; Translocation, Genetic
    Chemical Substances Magnesium (I38ZP9992A) ; MRS2 protein, human
    Language English
    Publishing date 2023-11-08
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-42599-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    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.

  2. Article: Cryo-EM structures of human magnesium channel MRS2 reveal gating and regulatory mechanisms.

    Lai, Louis Tung Faat / Balaraman, Jayashree / Zhou, Fei / Matthies, Doreen

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Magnesium ions ( ... ...

    Abstract Magnesium ions (Mg
    Language English
    Publishing date 2023-08-23
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.08.22.553867
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    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.

  3. Article ; Online: Lipid flipping in the omega-3 fatty-acid transporter.

    Nguyen, Chi / Lei, Hsiang-Ting / Lai, Louis Tung Faat / Gallenito, Marc J / Mu, Xuelang / Matthies, Doreen / Gonen, Tamir

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 2571

    Abstract: Mfsd2a is the transporter for docosahexaenoic acid (DHA), an omega-3 fatty acid, across the blood brain barrier (BBB). Defects in Mfsd2a are linked to ailments from behavioral and motor dysfunctions to microcephaly. Mfsd2a transports long-chain ... ...

    Abstract Mfsd2a is the transporter for docosahexaenoic acid (DHA), an omega-3 fatty acid, across the blood brain barrier (BBB). Defects in Mfsd2a are linked to ailments from behavioral and motor dysfunctions to microcephaly. Mfsd2a transports long-chain unsaturated fatty-acids, including DHA and α-linolenic acid (ALA), that are attached to the zwitterionic lysophosphatidylcholine (LPC) headgroup. Even with the recently determined structures of Mfsd2a, the molecular details of how this transporter performs the energetically unfavorable task of translocating and flipping lysolipids across the lipid bilayer remains unclear. Here, we report five single-particle cryo-EM structures of Danio rerio Mfsd2a (drMfsd2a): in the inward-open conformation in the ligand-free state and displaying lipid-like densities modeled as ALA-LPC at four distinct positions. These Mfsd2a snapshots detail the flipping mechanism for lipid-LPC from outer to inner membrane leaflet and release for membrane integration on the cytoplasmic side. These results also map Mfsd2a mutants that disrupt lipid-LPC transport and are associated with disease.
    MeSH term(s) Fatty Acids, Omega-3 ; Symporters/metabolism ; Membrane Transport Proteins/metabolism ; Blood-Brain Barrier/metabolism ; Biological Transport ; Docosahexaenoic Acids ; Lysophosphatidylcholines/chemistry
    Chemical Substances Fatty Acids, Omega-3 ; Symporters ; Membrane Transport Proteins ; Docosahexaenoic Acids (25167-62-8) ; Lysophosphatidylcholines
    Language English
    Publishing date 2023-05-08
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-37702-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    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.

  4. Article ; Online: SRPK2 Mediates HBV Core Protein Phosphorylation and Capsid Assembly via Docking Interaction.

    Yip, Ryan Pak Hong / Kwok, Doris Ching Ying / Lai, Louis Tung Faat / Ho, Siu-Ming / Wong, Ivan Chun Kit / Chan, Chi-Ping / Lau, Wilson Chun Yu / Ngo, Jacky Chi Ki

    PLoS pathogens

    2024  Volume 20, Issue 2, Page(s) e1011978

    Abstract: Members of the serine-arginine protein kinase (SRPK) family, SRPK1 and SRPK2, phosphorylate the hepatitis B core protein (Cp) and are crucial for pregenomic RNA encapsidation during viral nucleocapsid assembly. Among them, SRPK2 exhibits higher kinase ... ...

    Abstract Members of the serine-arginine protein kinase (SRPK) family, SRPK1 and SRPK2, phosphorylate the hepatitis B core protein (Cp) and are crucial for pregenomic RNA encapsidation during viral nucleocapsid assembly. Among them, SRPK2 exhibits higher kinase activity toward Cp. In this study, we identified Cp sites that are phosphorylated by SRPK2 and demonstrated that the kinase utilizes an SRPK-specific docking groove to interact with and regulate the phosphorylation of the C-terminal arginine rich domain of Cp. We determined that direct interaction between the docking groove of SRPK2 and unphosphorylated Cp inhibited premature viral capsid assembly in vitro, whereas the phosphorylation of the viral protein reactivated the process. Pull-down assays together with the new cryo-electron microscopy structure of the HBV capsid in complex with SRPK2 revealed that the kinases decorate the surface of the viral capsid by interacting with the C-terminal domain of Cp, underscoring the importance of the docking interaction in regulating capsid assembly and pregenome packaging. Moreover, SRPK2-knockout in HepG2 cells suppressed Cp phosphorylation, indicating that SRPK2 is an important cellular kinase for HBV life cycle.
    MeSH term(s) Phosphorylation ; Capsid/metabolism ; Hepatitis B virus/metabolism ; Cryoelectron Microscopy ; Protein Serine-Threonine Kinases/metabolism ; Capsid Proteins/metabolism ; Virus Assembly/physiology ; Arginine/metabolism
    Chemical Substances Protein Serine-Threonine Kinases (EC 2.7.11.1) ; Capsid Proteins ; Arginine (94ZLA3W45F)
    Language English
    Publishing date 2024-02-07
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1011978
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    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.

  5. Article ; Online: Structural Biology and Electron Microscopy of the Autophagy Molecular Machinery.

    Lai, Louis Tung Faat / Ye, Hao / Zhang, Wenxin / Jiang, Liwen / Lau, Wilson Chun Yu

    Cells

    2019  Volume 8, Issue 12

    Abstract: Autophagy is a highly regulated bulk degradation process that plays a key role in the maintenance of cellular homeostasis. During autophagy, a double membrane-bound compartment termed the autophagosome is formed through de novo nucleation and assembly of ...

    Abstract Autophagy is a highly regulated bulk degradation process that plays a key role in the maintenance of cellular homeostasis. During autophagy, a double membrane-bound compartment termed the autophagosome is formed through de novo nucleation and assembly of membrane sources to engulf unwanted cytoplasmic components and targets them to the lysosome or vacuole for degradation. Central to this process are the autophagy-related (ATG) proteins, which play a critical role in plant fitness, immunity, and environmental stress response. Over the past few years, cryo-electron microscopy (cryo-EM) and single-particle analysis has matured into a powerful and versatile technique for the structural determination of protein complexes at high resolution and has contributed greatly to our current understanding of the molecular mechanisms underlying autophagosome biogenesis. Here we describe the plant-specific ATG proteins and summarize recent structural and mechanistic studies on the protein machinery involved in autophagy initiation with an emphasis on those by single-particle analysis.
    MeSH term(s) Autophagosomes/metabolism ; Autophagosomes/ultrastructure ; Autophagy ; Autophagy-Related Proteins/chemistry ; Autophagy-Related Proteins/metabolism ; Microscopy, Electron ; Models, Molecular ; Plant Proteins/chemistry ; Plant Proteins/metabolism ; Plants/metabolism ; Plants/ultrastructure
    Chemical Substances Autophagy-Related Proteins ; Plant Proteins
    Language English
    Publishing date 2019-12-12
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells8121627
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    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.

  6. Article ; Online: Subnanometer resolution cryo-EM structure of

    Lai, Louis Tung Faat / Yu, Chuanyang / Wong, Jan Siu Kei / Lo, Ho Sing / Benlekbir, Samir / Jiang, Liwen / Lau, Wilson Chun Yu

    Autophagy

    2019  Volume 16, Issue 3, Page(s) 575–583

    Abstract: Macroautophagy/autophagy is an essential process for the maintenance of cellular homeostasis by recycling macromolecules under normal and stress conditions. ATG9 (autophagy related 9) is the only integral membrane protein in the autophagy core machinery ... ...

    Abstract Macroautophagy/autophagy is an essential process for the maintenance of cellular homeostasis by recycling macromolecules under normal and stress conditions. ATG9 (autophagy related 9) is the only integral membrane protein in the autophagy core machinery and has a central role in mediating autophagosome formation. In cells, ATG9 exists on mobile vesicles that traffic to the growing phagophore, providing an essential membrane source for the formation of autophagosomes. Here we report the three-dimensional structure of ATG9 from
    MeSH term(s) Arabidopsis/metabolism ; Arabidopsis/ultrastructure ; Arabidopsis Proteins/metabolism ; Arabidopsis Proteins/ultrastructure ; Autophagy-Related Proteins/metabolism ; Autophagy-Related Proteins/ultrastructure ; Cryoelectron Microscopy ; Membrane Proteins/metabolism ; Membrane Proteins/ultrastructure ; Models, Molecular ; Nanotechnology ; Protein Multimerization ; Protein Structure, Secondary ; Structural Homology, Protein
    Chemical Substances APG9 protein, Arabidopsis ; Arabidopsis Proteins ; Autophagy-Related Proteins ; Membrane Proteins
    Language English
    Publishing date 2019-07-16
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.1080/15548627.2019.1639300
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 6741: 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

    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.

  7. Article ; Online: Structural basis of substrate recognition and thermal protection by a small heat shock protein.

    Yu, Chuanyang / Leung, Stephen King Pong / Zhang, Wenxin / Lai, Louis Tung Faat / Chan, Ying Ki / Wong, Man Chit / Benlekbir, Samir / Cui, Yong / Jiang, Liwen / Lau, Wilson Chun Yu

    Nature communications

    2021  Volume 12, Issue 1, Page(s) 3007

    Abstract: Small heat shock proteins (sHsps) bind unfolding proteins, thereby playing a pivotal role in the maintenance of proteostasis in virtually all living organisms. Structural elucidation of sHsp-substrate complexes has been hampered by the transient and ... ...

    Abstract Small heat shock proteins (sHsps) bind unfolding proteins, thereby playing a pivotal role in the maintenance of proteostasis in virtually all living organisms. Structural elucidation of sHsp-substrate complexes has been hampered by the transient and heterogeneous nature of their interactions, and the precise mechanisms underlying substrate recognition, promiscuity, and chaperone activity of sHsps remain unclear. Here we show the formation of a stable complex between Arabidopsis thaliana plastid sHsp, Hsp21, and its natural substrate 1-deoxy-D-xylulose 5-phosphate synthase (DXPS) under heat stress, and report cryo-electron microscopy structures of Hsp21, DXPS and Hsp21-DXPS complex at near-atomic resolution. Monomeric Hsp21 binds across the dimer interface of DXPS and engages in multivalent interactions by recognizing highly dynamic structural elements in DXPS. Hsp21 partly unfolds its central α-crystallin domain to facilitate binding of DXPS, which preserves a native-like structure. This mode of interaction suggests a mechanism of sHsps anti-aggregation activity towards a broad range of substrates.
    MeSH term(s) Arabidopsis/genetics ; Arabidopsis/metabolism ; Arabidopsis Proteins/metabolism ; Cryoelectron Microscopy ; Heat-Shock Proteins/chemistry ; Heat-Shock Proteins/metabolism ; Heat-Shock Proteins, Small/chemistry ; Heat-Shock Proteins, Small/genetics ; Heat-Shock Proteins, Small/metabolism ; Heat-Shock Response ; Models, Molecular ; Protein Folding ; Transferases/chemistry ; Transferases/metabolism
    Chemical Substances Arabidopsis Proteins ; HSP21 protein, Arabidopsis ; Heat-Shock Proteins ; Heat-Shock Proteins, Small ; Transferases (EC 2.-) ; deoxyxylulose-5-phosphate synthase (EC 2.2.1.-)
    Language English
    Publishing date 2021-05-21
    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/s41467-021-23338-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    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.

  8. Article ; Online: MTV proteins unveil ER- and microtubule-associated compartments in the plant vacuolar trafficking pathway.

    Delgadillo, María Otilia / Ruano, Guillermo / Zouhar, Jan / Sauer, Michael / Shen, Jinbo / Lazarova, Aleksandra / Sanmartín, Maite / Lai, Louis Tung Faat / Deng, Cesi / Wang, Pengwei / Hussey, Patrick J / Sánchez-Serrano, José Juan / Jiang, Liwen / Rojo, Enrique

    Proceedings of the National Academy of Sciences of the United States of America

    2020  Volume 117, Issue 18, Page(s) 9884–9895

    Abstract: The factors and mechanisms involved in vacuolar transport in plants, and in particular those directing vesicles to their target endomembrane compartment, remain largely unknown. To identify components of the vacuolar trafficking machinery, we searched ... ...

    Abstract The factors and mechanisms involved in vacuolar transport in plants, and in particular those directing vesicles to their target endomembrane compartment, remain largely unknown. To identify components of the vacuolar trafficking machinery, we searched for
    MeSH term(s) Alleles ; Arabidopsis/genetics ; Arabidopsis/metabolism ; Arabidopsis Proteins/genetics ; Arabidopsis Proteins/metabolism ; Cytoplasmic Vesicles/genetics ; Cytoplasmic Vesicles/metabolism ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/genetics ; Golgi Apparatus/metabolism ; Kinesin/genetics ; Kinesin/metabolism ; Microtubules/genetics ; Microtubules/metabolism ; Multivesicular Bodies/genetics ; Multivesicular Bodies/metabolism ; Mutation ; Protein Transport/genetics ; Vacuoles/genetics ; Vacuoles/metabolism ; Vesicular Transport Proteins/genetics ; Vesicular Transport Proteins/metabolism
    Chemical Substances Arabidopsis Proteins ; Vesicular Transport Proteins ; Kinesin (EC 3.6.4.4)
    Language English
    Publishing date 2020-04-22
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1919820117
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: 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

    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.

  9. Article ; Online: Modular enzyme assembly for enhanced cascade biocatalysis and metabolic flux.

    Kang, Wei / Ma, Tian / Liu, Min / Qu, Jiale / Liu, Zhenjun / Zhang, Huawei / Shi, Bin / Fu, Shuai / Ma, Juncai / Lai, Louis Tung Faat / He, Sicong / Qu, Jianan / Wing-Ngor Au, Shannon / Ho Kang, Byung / Yu Lau, Wilson Chun / Deng, Zixin / Xia, Jiang / Liu, Tiangang

    Nature communications

    2019  Volume 10, Issue 1, Page(s) 4248

    Abstract: Enzymatic reactions in living cells are highly dynamic but simultaneously tightly regulated. Enzyme engineers seek to construct multienzyme complexes to prevent intermediate diffusion, to improve product yield, and to control the flux of metabolites. ... ...

    Abstract Enzymatic reactions in living cells are highly dynamic but simultaneously tightly regulated. Enzyme engineers seek to construct multienzyme complexes to prevent intermediate diffusion, to improve product yield, and to control the flux of metabolites. Here we choose a pair of short peptide tags (RIAD and RIDD) to create scaffold-free enzyme assemblies to achieve these goals. In vitro, assembling enzymes in the menaquinone biosynthetic pathway through RIAD-RIDD interaction yields protein nanoparticles with varying stoichiometries, sizes, geometries, and catalytic efficiency. In Escherichia coli, assembling the last enzyme of the upstream mevalonate pathway with the first enzyme of the downstream carotenoid pathway leads to the formation of a pathway node, which increases carotenoid production by 5.7 folds. The same strategy results in a 58% increase in lycopene production in engineered Saccharomyces cerevisiae. This work presents a simple strategy to impose metabolic control in biosynthetic microbe factories.
    MeSH term(s) Biocatalysis ; Bioreactors/microbiology ; Biosynthetic Pathways/genetics ; Carotenoids/metabolism ; Escherichia coli/enzymology ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Lycopene/metabolism ; Metabolic Engineering/methods ; Mevalonic Acid/metabolism ; Protein Engineering/methods ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Vitamin K 2/metabolism
    Chemical Substances Vitamin K 2 (11032-49-8) ; Carotenoids (36-88-4) ; Mevalonic Acid (S5UOB36OCZ) ; Lycopene (SB0N2N0WV6)
    Language English
    Publishing date 2019-09-18
    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/s41467-019-12247-w
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    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.

To top