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  1. Article ; Online: How cells flex their PEX to fine-tune lipolysis in NAFLD.

    Paul, Blessy / Henne, W Mike

    Nature metabolism

    2021  Volume 3, Issue 12, Page(s) 1591–1593

    Language English
    Publishing date 2021-12-13
    Publishing country Germany
    Document type Journal Article
    ISSN 2522-5812
    ISSN (online) 2522-5812
    DOI 10.1038/s42255-021-00490-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Spatial proteomics of ER tubules reveals CLMN, an ER-actin tether at focal adhesions that promotes cell migration.

    Merta, Holly / Isogai, Tadamoto / Paul, Blessy / Danuser, Gaudenz / Henne, W Mike

    bioRxiv : the preprint server for biology

    2024  

    Abstract: The endoplasmic reticulum (ER) is structurally and functionally diverse, yet how its functions are organized within morphological subdomains is incompletely understood. Utilizing TurboID-based proximity labeling and CRISPR knock-in technologies, here we ... ...

    Abstract The endoplasmic reticulum (ER) is structurally and functionally diverse, yet how its functions are organized within morphological subdomains is incompletely understood. Utilizing TurboID-based proximity labeling and CRISPR knock-in technologies, here we map the proteomic landscape of the human ER and nuclear envelope. Spatial proteomics reveals enrichments of proteins into ER tubules, sheets, and nuclear envelope. We uncover an ER-enriched actin-binding protein, Calmin (CLMN), and define it as an ER-actin tether that localizes to focal adhesions adjacent to ER tubules. CLMN depletion perturbs focal adhesion disassembly, actin dynamics, and cell movement. Mechanistically, CLMN-depleted cells also exhibit defects in calcium signaling near ER-actin interfaces, suggesting CLMN promotes calcium signaling near adhesions to facilitate their disassembly. Collectively, we map the sub-organelle proteome landscape of the ER, identify CLMN as an ER-actin tether, and describe a non-canonical mechanism by which ER tubules engage actin to regulate cell migration.
    Language English
    Publishing date 2024-01-25
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.01.24.577043
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: The fat body cortical actin network regulates

    Ugrankar-Banerjee, Rupali / Tran, Son / Bowerman, Jade / Kovalenko, Anastasiia / Paul, Blessy / Henne, W Mike

    eLife

    2023  Volume 12

    Abstract: Defective nutrient storage and adipocyte enlargement (hypertrophy) are emerging features of metabolic syndrome and type 2 diabetes. Within adipose tissues, how the cytoskeletal network contributes to adipose cell size, nutrient uptake, fat storage, and ... ...

    Abstract Defective nutrient storage and adipocyte enlargement (hypertrophy) are emerging features of metabolic syndrome and type 2 diabetes. Within adipose tissues, how the cytoskeletal network contributes to adipose cell size, nutrient uptake, fat storage, and signaling remain poorly understood. Utilizing the
    MeSH term(s) Animals ; Actins/metabolism ; Adipocytes/metabolism ; Adipose Tissue/metabolism ; Diabetes Mellitus, Type 2/metabolism ; Drosophila/metabolism ; Fat Body/metabolism ; Lipids ; Nutrients
    Chemical Substances Actins ; Lipids ; Act5C protein, Drosophila
    Language English
    Publishing date 2023-05-05
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.81170
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  4. Article ; Online: Recognising the signals for endosomal trafficking.

    Weeratunga, Saroja / Paul, Blessy / Collins, Brett M

    Current opinion in cell biology

    2020  Volume 65, Page(s) 17–27

    Abstract: The endosomal compartment is a major sorting station controlling the balance between endocytic recycling and lysosomal degradation, and its homeostasis is emerging as a central factor in various neurodegenerative diseases such as Alzheimer's and ... ...

    Abstract The endosomal compartment is a major sorting station controlling the balance between endocytic recycling and lysosomal degradation, and its homeostasis is emerging as a central factor in various neurodegenerative diseases such as Alzheimer's and Parkinson's. Membrane trafficking is generally coordinated by the recognition of specific signals in transmembrane protein cargos by different transport machineries. A number of different protein trafficking complexes are essential for sequence-specific recognition and retrieval of endosomal cargos, recycling them to other compartments and acting to counter-balance the default endosomal sorting complex required for transport-mediated degradation pathway. In this review, we provide a summary of the key endosomal transport machineries, and the molecular mechanisms by which different cargo sequences are specifically recognised.
    MeSH term(s) Endosomal Sorting Complexes Required for Transport/metabolism ; Endosomes/metabolism ; Humans ; Lysosomes/metabolism ; Signal Transduction ; Sorting Nexins/metabolism ; Ubiquitination
    Chemical Substances Endosomal Sorting Complexes Required for Transport ; Sorting Nexins
    Language English
    Publishing date 2020-03-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1026381-0
    ISSN 1879-0410 ; 0955-0674
    ISSN (online) 1879-0410
    ISSN 0955-0674
    DOI 10.1016/j.ceb.2020.02.005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Structural Predictions of the SNX-RGS Proteins Suggest They Belong to a New Class of Lipid Transfer Proteins.

    Paul, Blessy / Weeratunga, Saroja / Tillu, Vikas A / Hariri, Hanaa / Henne, W Mike / Collins, Brett M

    Frontiers in cell and developmental biology

    2022  Volume 10, Page(s) 826688

    Abstract: Recent advances in protein structure prediction using machine learning such as AlphaFold2 and RosettaFold presage a revolution in structural biology. Genome-wide predictions of protein structures are providing unprecedented insights into their ... ...

    Abstract Recent advances in protein structure prediction using machine learning such as AlphaFold2 and RosettaFold presage a revolution in structural biology. Genome-wide predictions of protein structures are providing unprecedented insights into their architecture and intradomain interactions, and applications have already progressed towards assessing protein complex formation. Here we present detailed analyses of the sorting nexin proteins that contain regulator of G-protein signalling domains (SNX-RGS proteins), providing a key example of the ability of AlphaFold2 to reveal novel structures with previously unsuspected biological functions. These large proteins are conserved in most eukaryotes and are known to associate with lipid droplets (LDs) and sites of LD-membrane contacts, with key roles in regulating lipid metabolism. They possess five domains, including an N-terminal transmembrane domain that anchors them to the endoplasmic reticulum, an RGS domain, a lipid interacting phox homology (PX) domain and two additional domains named the PXA and PXC domains of unknown structure and function. Here we report the crystal structure of the RGS domain of sorting nexin 25 (SNX25) and show that the AlphaFold2 prediction closely matches the experimental structure. Analysing the full-length SNX-RGS proteins across multiple homologues and species we find that the distant PXA and PXC domains in fact fold into a single unique structure that notably features a large and conserved hydrophobic pocket. The nature of this pocket strongly suggests a role in lipid or fatty acid binding, and we propose that these molecules represent a new class of conserved lipid transfer proteins.
    Language English
    Publishing date 2022-02-03
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2022.826688
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  6. Article: Paraoxonase-like APMAP maintains endoplasmic reticulum-associated lipid and lipoprotein homeostasis.

    Paul, Blessy / Merta, Holly / Ugrankar-Banerjee, Rupali / Hensley, Monica / Tran, Son / Dias do Vale, Goncalo / McDonald, Jeffrey G / Farber, Steven A / Henne, W Mike

    bioRxiv : the preprint server for biology

    2024  

    Abstract: Oxidative stress perturbs lipid homeostasis and contributes to metabolic diseases. Though ignored compared to mitochondrial oxidation, the endoplasmic reticulum (ER) generates reactive oxygen species requiring antioxidant quality control. Using multi- ... ...

    Abstract Oxidative stress perturbs lipid homeostasis and contributes to metabolic diseases. Though ignored compared to mitochondrial oxidation, the endoplasmic reticulum (ER) generates reactive oxygen species requiring antioxidant quality control. Using multi-organismal profiling featuring
    Language English
    Publishing date 2024-01-27
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2024.01.26.577049
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Escherichia coli Protein Expression System for Acetylcholine Binding Proteins (AChBPs).

    Abraham, Nikita / Paul, Blessy / Ragnarsson, Lotten / Lewis, Richard J

    PloS one

    2016  Volume 11, Issue 6, Page(s) e0157363

    Abstract: Nicotinic acetylcholine receptors (nAChR) are ligand gated ion channels, identified as therapeutic targets for a range of human diseases. Drug design for nAChR related disorders is increasingly using structure-based approaches. Many of these structural ... ...

    Abstract Nicotinic acetylcholine receptors (nAChR) are ligand gated ion channels, identified as therapeutic targets for a range of human diseases. Drug design for nAChR related disorders is increasingly using structure-based approaches. Many of these structural insights for therapeutic lead development have been obtained from co-crystal structures of nAChR agonists and antagonists with the acetylcholine binding protein (AChBP). AChBP is a water soluble, structural and functional homolog of the extracellular, ligand-binding domain of nAChRs. Currently, AChBPs are recombinantly expressed in eukaryotic expression systems for structural and biophysical studies. Here, we report the establishment of an Escherichia coli (E. coli) expression system that significantly reduces the cost and time of production compared to the existing expression systems. E. coli can efficiently express unglycosylated AChBP for crystallography and makes the expression of isotopically labelled forms feasible for NMR. We used a pHUE vector containing an N-terminal His-tagged ubiquitin fusion protein to facilitate AChBP expression in the soluble fractions, and thus avoid the need to recover protein from inclusion bodies. The purified protein yield obtained from the E. coli expression system is comparable to that obtained from existing AChBP expression systems. E. coli expressed AChBP bound nAChR agonists and antagonists with affinities matching those previously reported. Thus, the E. coli expression system significantly simplifies the expression and purification of functional AChBP for structural and biophysical studies.
    MeSH term(s) Acetylcholine/metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/chemistry ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Crystallography, X-Ray ; Escherichia coli/genetics ; Gene Expression ; Genetic Vectors/genetics ; Humans ; Ligands ; Pichia/genetics ; Protein Binding ; Receptors, Nicotinic/chemistry ; Receptors, Nicotinic/genetics ; Receptors, Nicotinic/metabolism ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism
    Chemical Substances AChBP protein, Lymnaea ; Carrier Proteins ; Ligands ; Receptors, Nicotinic ; Recombinant Fusion Proteins ; Acetylcholine (N9YNS0M02X)
    Language English
    Publishing date 2016-06-15
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2267670-3
    ISSN 1932-6203 ; 1932-6203
    ISSN (online) 1932-6203
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0157363
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  8. Article ; Online: Structural basis for the hijacking of endosomal sorting nexin proteins by

    Paul, Blessy / Kim, Hyun Sung / Kerr, Markus C / Huston, Wilhelmina M / Teasdale, Rohan D / Collins, Brett M

    eLife

    2017  Volume 6

    Abstract: During infection chlamydial pathogens form an intracellular membrane-bound replicative niche termed the inclusion, which is enriched with bacterial transmembrane proteins called Incs. Incs bind and manipulate host cell proteins to promote inclusion ... ...

    Abstract During infection chlamydial pathogens form an intracellular membrane-bound replicative niche termed the inclusion, which is enriched with bacterial transmembrane proteins called Incs. Incs bind and manipulate host cell proteins to promote inclusion expansion and provide camouflage against innate immune responses. Sorting nexin (SNX) proteins that normally function in endosomal membrane trafficking are a major class of inclusion-associated host proteins, and are recruited by IncE/CT116. Crystal structures of the SNX5 phox-homology (PX) domain in complex with IncE define the precise molecular basis for these interactions. The binding site is unique to SNX5 and related family members SNX6 and SNX32. Intriguingly the site is also conserved in SNX5 homologues throughout evolution, suggesting that IncE captures SNX5-related proteins by mimicking a native host protein interaction. These findings thus provide the first mechanistic insights both into how chlamydial Incs hijack host proteins, and how SNX5-related PX domains function as scaffolds in protein complex assembly.
    Language English
    Publishing date 2017-02-22
    Publishing country England
    Document type Journal Article
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.22311
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  9. Article ; Online: Molecular identification of a BAR domain-containing coat complex for endosomal recycling of transmembrane proteins.

    Simonetti, Boris / Paul, Blessy / Chaudhari, Karina / Weeratunga, Saroja / Steinberg, Florian / Gorla, Madhavi / Heesom, Kate J / Bashaw, Greg J / Collins, Brett M / Cullen, Peter J

    Nature cell biology

    2019  Volume 21, Issue 10, Page(s) 1219–1233

    Abstract: Protein trafficking requires coat complexes that couple recognition of sorting motifs in transmembrane cargoes with biogenesis of transport carriers. The mechanisms of cargo transport through the endosomal network are poorly understood. Here, we identify ...

    Abstract Protein trafficking requires coat complexes that couple recognition of sorting motifs in transmembrane cargoes with biogenesis of transport carriers. The mechanisms of cargo transport through the endosomal network are poorly understood. Here, we identify a sorting motif for endosomal recycling of cargoes, including the cation-independent mannose-6-phosphate receptor and semaphorin 4C, by the membrane tubulating BAR domain-containing sorting nexins SNX5 and SNX6. Crystal structures establish that this motif folds into a β-hairpin, which binds a site in the SNX5/SNX6 phox homology domains. Over sixty cargoes share this motif and require SNX5/SNX6 for their recycling. These include cargoes involved in neuronal migration and a Drosophila snx6 mutant displays defects in axonal guidance. These studies identify a sorting motif and provide molecular insight into an evolutionary conserved coat complex, the 'Endosomal SNX-BAR sorting complex for promoting exit 1' (ESCPE-1), which couples sorting motif recognition to the BAR-domain-mediated biogenesis of cargo-enriched tubulo-vesicular transport carriers.
    MeSH term(s) Amino Acid Motifs/genetics ; Animals ; Drosophila melanogaster ; Endosomes/metabolism ; HEK293 Cells ; HeLa Cells ; Humans ; Membrane Proteins/metabolism ; Protein Domains/genetics ; Protein Transport/physiology ; Receptor, IGF Type 2/chemistry ; Receptor, IGF Type 2/metabolism ; Semaphorins/genetics ; Semaphorins/metabolism ; Sorting Nexins/chemistry ; Sorting Nexins/genetics ; Sorting Nexins/metabolism
    Chemical Substances Membrane Proteins ; Receptor, IGF Type 2 ; SNX5 protein, human ; SNX6 protein, human ; Semaphorins ; Sorting Nexins
    Language English
    Publishing date 2019-10-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1474722-4
    ISSN 1476-4679 ; 1465-7392
    ISSN (online) 1476-4679
    ISSN 1465-7392
    DOI 10.1038/s41556-019-0393-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5169: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 12: Show issues

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  10. Article ; Online: Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities.

    Chandra, Mintu / Chin, Yanni K-Y / Mas, Caroline / Feathers, J Ryan / Paul, Blessy / Datta, Sanchari / Chen, Kai-En / Jia, Xinying / Yang, Zhe / Norwood, Suzanne J / Mohanty, Biswaranjan / Bugarcic, Andrea / Teasdale, Rohan D / Henne, W Mike / Mobli, Mehdi / Collins, Brett M

    Nature communications

    2019  Volume 10, Issue 1, Page(s) 1528

    Abstract: Phox homology (PX) domains are membrane interacting domains that bind to phosphatidylinositol phospholipids or phosphoinositides, markers of organelle identity in the endocytic system. Although many PX domains bind the canonical endosome-enriched lipid ... ...

    Abstract Phox homology (PX) domains are membrane interacting domains that bind to phosphatidylinositol phospholipids or phosphoinositides, markers of organelle identity in the endocytic system. Although many PX domains bind the canonical endosome-enriched lipid PtdIns3P, others interact with alternative phosphoinositides, and a precise understanding of how these specificities arise has remained elusive. Here we systematically screen all human PX domains for their phospholipid preferences using liposome binding assays, biolayer interferometry and isothermal titration calorimetry. These analyses define four distinct classes of human PX domains that either bind specifically to PtdIns3P, non-specifically to various di- and tri-phosphorylated phosphoinositides, bind both PtdIns3P and other phosphoinositides, or associate with none of the lipids tested. A comprehensive evaluation of PX domain structures reveals two distinct binding sites that explain these specificities, providing a basis for defining and predicting the functional membrane interactions of the entire PX domain protein family.
    MeSH term(s) Binding Sites ; Calorimetry ; Humans ; Interferometry ; Models, Molecular ; Phosphatidylinositols/chemistry ; Phosphatidylinositols/metabolism ; Protein Domains ; Sequence Analysis, Protein ; Sorting Nexins/chemistry ; Sorting Nexins/metabolism
    Chemical Substances Phosphatidylinositols ; SNX25 protein, human ; Sorting Nexins
    Language English
    Publishing date 2019-04-04
    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/s41467-019-09355-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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