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  1. Article: Syndapin Regulates the RAP-1 GTPase to Control Endocytic Recycling via RHO-1 and Non-Muscle Myosin II.

    Rodriguez-Polanco, Wilmer R / Norris, Anne / Velasco, Agustin B / Gleason, Adenrele M / Grant, Barth D

    bioRxiv : the preprint server for biology

    2023  

    Abstract: After endocytosis, many plasma membrane components are recycled via narrow-diameter membrane tubules that emerge from early endosomes to form recycling endosomes, eventually leading to their return to the plasma membrane. We previously showed that the F- ... ...

    Abstract After endocytosis, many plasma membrane components are recycled via narrow-diameter membrane tubules that emerge from early endosomes to form recycling endosomes, eventually leading to their return to the plasma membrane. We previously showed that the F-BAR and SH3 domain Syndapin/PACSIN-family protein SDPN-1 is required
    Language English
    Publishing date 2023-02-28
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.02.27.530328
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Endosomal microdomains: Formation and function.

    Norris, Anne / Grant, Barth D

    Current opinion in cell biology

    2020  Volume 65, Page(s) 86–95

    Abstract: It is widely recognized that after endocytosis, internalized cargo is delivered to endosomes that act as sorting stations. The limiting membrane of endosomes contain specialized subregions, or microdomains, that represent distinct functions of the ... ...

    Abstract It is widely recognized that after endocytosis, internalized cargo is delivered to endosomes that act as sorting stations. The limiting membrane of endosomes contain specialized subregions, or microdomains, that represent distinct functions of the endosome, including regions competing for cargo capture leading to degradation or recycling. Great progress has been made in defining the endosomal protein coats that sort cargo in these domains, including Retromer that recycles transmembrane cargo, and ESCRT (endosomal sorting complex required for transport) that degrades transmembrane cargo. In this review, we discuss recent work that is beginning to unravel how such coat complexes contribute to the creation and maintenance of endosomal microdomains. We highlight data that indicates that adjacent microdomains do not act independently but rather interact to cross-regulate. We posit that these interactions provide an agile means for the cell to adjust sorting in response to extracellular signals and intracellular metabolic cues.
    MeSH term(s) Actins/metabolism ; Animals ; Endosomes/metabolism ; Humans ; Membrane Microdomains/metabolism ; Membrane Proteins/metabolism ; Protein Transport ; Ubiquitination
    Chemical Substances Actins ; Membrane Proteins
    Language English
    Publishing date 2020-04-01
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 1026381-0
    ISSN 1879-0410 ; 0955-0674
    ISSN (online) 1879-0410
    ISSN 0955-0674
    DOI 10.1016/j.ceb.2020.02.018
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2963: Show issues Location:
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  3. Article: A Conserved Requirement for RME-8/DNAJC13 in Neuronal Autolysosome Reformation.

    Swords, Sierra / Jia, Nuo / Norris, Anne / Modi, Jil / Cai, Qian / Grant, Barth D

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Autophagosomes fuse with lysosomes, forming autolysosomes that degrade engulfed cargo. To maintain lysosomal capacity, autolysosome reformation (ALR) must regenerate lysosomes from autolysosomes using a membrane tubule-based process. Maintaining ... ...

    Abstract Autophagosomes fuse with lysosomes, forming autolysosomes that degrade engulfed cargo. To maintain lysosomal capacity, autolysosome reformation (ALR) must regenerate lysosomes from autolysosomes using a membrane tubule-based process. Maintaining lysosomal capacity is required to maintain proteostasis and cellular health, especially in neurons where lysosomal dysfunction has been repeatedly implicated in neurodegenerative disease. Cell biological studies have linked the DNA-J domain Hsc70 co-chaperone RME-8/DNAJC13 to endosomal coat protein regulation, while human genetics studies have linked RME-8/DNAJC13 to neurological disease, including Parkinsonism and Essential Tremor. We report new analysis of the requirements for the RME-8/DNAJC13 protein in neurons, focusing on
    Language English
    Publishing date 2023-02-28
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.02.27.530319
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: A conserved requirement for RME-8/DNAJC13 in neuronal autophagic lysosome reformation.

    Swords, Sierra B / Jia, Nuo / Norris, Anne / Modi, Jil / Cai, Qian / Grant, Barth D

    Autophagy

    2023  , Page(s) 1–17

    Abstract: Autophagosomes fuse with lysosomes, forming autolysosomes that degrade engulfed cargo. To maintain lysosomal capacity, autophagic lysosome reformation (ALR) must regenerate lysosomes from autolysosomes using a membrane tubule-based process. Maintaining ... ...

    Abstract Autophagosomes fuse with lysosomes, forming autolysosomes that degrade engulfed cargo. To maintain lysosomal capacity, autophagic lysosome reformation (ALR) must regenerate lysosomes from autolysosomes using a membrane tubule-based process. Maintaining lysosomal capacity is required to maintain cellular health, especially in neurons where lysosomal dysfunction has been repeatedly implicated in neurodegenerative disease. The DNA-J domain HSC70 co-chaperone RME-8/DNAJC13 has been linked to endosomal coat protein regulation and to neurological disease. We report new analysis of the requirements for the RME-8/DNAJC13 protein in neurons, focusing on intact
    Language English
    Publishing date 2023-11-09
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.1080/15548627.2023.2269028
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 6741: Show issues Location:
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  5. Article: Active zone protein SYD-2/Liprin-

    Nadiminti, Sravanthi S P / Dixit, Shirley B / Ratnakaran, Neena / Hegde, Sneha / Swords, Sierra / Grant, Barth D / Koushika, Sandhya P

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Synaptic vesicle proteins (SVps) are thought to travel in heterogeneous carriers dependent on the motor UNC-104/KIF1A. ... ...

    Abstract Synaptic vesicle proteins (SVps) are thought to travel in heterogeneous carriers dependent on the motor UNC-104/KIF1A. In
    Language English
    Publishing date 2023-02-26
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.02.26.530068
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Syndapin and GTPase RAP-1 control endocytic recycling via RHO-1 and non-muscle myosin II.

    Rodriguez-Polanco, Wilmer R / Norris, Anne / Velasco, Agustin B / Gleason, Adenrele M / Grant, Barth D

    Current biology : CB

    2023  Volume 33, Issue 22, Page(s) 4844–4856.e5

    Abstract: After endocytosis, many plasma membrane components are recycled via membrane tubules that emerge from early endosomes to form recycling endosomes, eventually leading to their return to the plasma membrane. We previously showed that Syndapin/PACSIN-family ...

    Abstract After endocytosis, many plasma membrane components are recycled via membrane tubules that emerge from early endosomes to form recycling endosomes, eventually leading to their return to the plasma membrane. We previously showed that Syndapin/PACSIN-family protein SDPN-1 is required in vivo for basolateral endocytic recycling in the C. elegans intestine. Here, we document an interaction between the SDPN-1 SH3 domain and a target sequence in PXF-1/PDZ-GEF1/RAPGEF2, a known exchange factor for Rap-GTPases. We found that endogenous mutations engineered into the SDPN-1 SH3 domain, or its binding site in the PXF-1 protein, interfere with recycling in vivo, as does the loss of the PXF-1 target RAP-1. In some contexts, Rap-GTPases negatively regulate RhoA activity, suggesting a potential for Syndapin to regulate RhoA. Our results indicate that in the C. elegans intestine, RHO-1/RhoA is enriched on SDPN-1- and RAP-1-positive endosomes, and the loss of SDPN-1 or RAP-1 elevates RHO-1(GTP) levels on intestinal endosomes. Furthermore, we found that depletion of RHO-1 suppressed sdpn-1 mutant recycling defects, indicating that control of RHO-1 activity is a key mechanism by which SDPN-1 acts to promote endocytic recycling. RHO-1/RhoA is well known for controlling actomyosin contraction cycles, although little is known about the effects of non-muscle myosin II on endosomes. Our analysis found that non-muscle myosin II is enriched on SDPN-1-positive endosomes, with two non-muscle myosin II heavy-chain isoforms acting in apparent opposition. Depletion of nmy-2 inhibited recycling like sdpn-1 mutants, whereas depletion of nmy-1 suppressed sdpn-1 mutant recycling defects, indicating that actomyosin contractility controls recycling endosome function.
    MeSH term(s) Animals ; Caenorhabditis elegans/genetics ; Caenorhabditis elegans/metabolism ; GTP Phosphohydrolases/metabolism ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Actomyosin/metabolism ; Endocytosis/physiology ; Endosomes/metabolism ; Myosin Type II/metabolism
    Chemical Substances GTP Phosphohydrolases (EC 3.6.1.-) ; Caenorhabditis elegans Proteins ; Actomyosin (9013-26-7) ; Myosin Type II (EC 3.6.1.-)
    Language English
    Publishing date 2023-10-12
    Publishing country England
    Document type Journal Article
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2023.09.051
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3208: Show issues Location:
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  7. Article ; Online: Mutagenesis and structural modeling implicate RME-8 IWN domains as conformational control points.

    Norris, Anne / McManus, Collin T / Wang, Simon / Ying, Ruochen / Grant, Barth D

    PLoS genetics

    2022  Volume 18, Issue 10, Page(s) e1010296

    Abstract: After endocytosis, transmembrane cargo is differentially sorted into degradative or recycling pathways. This process is facilitated by recruitment into physically distinct degradative or recycling microdomains on the limiting membrane of individual ... ...

    Abstract After endocytosis, transmembrane cargo is differentially sorted into degradative or recycling pathways. This process is facilitated by recruitment into physically distinct degradative or recycling microdomains on the limiting membrane of individual endosomes. Endosomal sorting complexes required for transport (ESCRT) mark the degradative microdomain, while the recycling domain is marked by the retromer complex and associated proteins RME-8 and SNX-1. The separation of endosomal microdomains is also controlled by RME-8 and SNX-1, at least in part via removal of degradative component HRS/HGRS-1 from the recycling microdomain. This activity is likely due to recruitment and activation of chaperone Hsc70 on the endosome by the RME-8 DNAJ domain. To better understand the mechanism of RME-8 function we performed a new phylogenetic analysis of RME-8 and identified new conserved sequence features. In a complementary approach, we performed structure-function analysis that identified the C-terminus as important for microdomain localization and likely substrate binding, while N-terminal sequences beyond the known single N-terminal PH-like domain are important for endosome recruitment. Random mutagenesis identified IWN4, and by analogy IWN3, to be important for the autoinhibitory DNAJ domain binding, with IWN3 playing a critical role in HRS uncoating activity. Combining AlphaFold structural predictions with in vivo mutation analysis of RME-8, we propose a model whereby SNX-1 and the IWN domains control the conformation of RME-8 and hence the productive exposure of the DNAJ domain. Furthermore, we propose that the activation of RME-8 is cyclical, with SNX-1 acting as an activator and a target of RME-8 uncoating activity.
    MeSH term(s) Phylogeny ; Endosomes/genetics ; Endosomes/metabolism ; Protein Transport ; Endocytosis ; Mutagenesis ; Sorting Nexins/genetics
    Chemical Substances Sorting Nexins
    Language English
    Publishing date 2022-10-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2186725-2
    ISSN 1553-7404 ; 1553-7390
    ISSN (online) 1553-7404
    ISSN 1553-7390
    DOI 10.1371/journal.pgen.1010296
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Mechanical force of uterine occupation enables large vesicle extrusion from proteostressed maternal neurons.

    Wang, Guoqiang / Guasp, Ryan / Salam, Sangeena / Chuang, Edward / Morera, Andrés / Smart, Anna J / Jimenez, David / Shekhar, Sahana / Melentijevic, Ilija / Nguyen, Ken C / Hall, David H / Grant, Barth D / Driscoll, Monica

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Large vesicle extrusion from neurons may contribute to spreading pathogenic protein aggregates and promoting inflammatory responses, two mechanisms leading to neurodegenerative disease. Factors that regulate extrusion of large vesicles, such as exophers ... ...

    Abstract Large vesicle extrusion from neurons may contribute to spreading pathogenic protein aggregates and promoting inflammatory responses, two mechanisms leading to neurodegenerative disease. Factors that regulate extrusion of large vesicles, such as exophers produced by proteostressed
    Language English
    Publishing date 2023-11-16
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.11.13.565361
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Large vesicle extrusions from

    Wang, Yu / Arnold, Meghan Lee / Smart, Anna Joelle / Wang, Guoqiang / Androwski, Rebecca J / Morera, Andres / Nguyen, Ken C Q / Schweinsberg, Peter J / Bai, Ge / Cooper, Jason / Hall, David H / Driscoll, Monica / Grant, Barth D

    eLife

    2023  Volume 12

    Abstract: Caenorhabditis ... ...

    Abstract Caenorhabditis elegans
    MeSH term(s) Animals ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/metabolism ; Neurodegenerative Diseases/metabolism ; Apoptosis/physiology ; Phagocytosis/physiology ; Phagosomes/metabolism ; Neurons/metabolism ; Neuroglia/metabolism ; Carrier Proteins/metabolism ; GTP Phosphohydrolases/metabolism ; Mammals/metabolism
    Chemical Substances Caenorhabditis elegans Proteins ; Carrier Proteins ; GTP Phosphohydrolases (EC 3.6.1.-)
    Language English
    Publishing date 2023-03-02
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.82227
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Stress increases in exopher-mediated neuronal extrusion require lipid biosynthesis, FGF, and EGF RAS/MAPK signaling.

    Cooper, Jason F / Guasp, Ryan J / Arnold, Meghan Lee / Grant, Barth D / Driscoll, Monica

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

    2021  Volume 118, Issue 36

    Abstract: In human neurodegenerative diseases, neurons can transfer toxic protein aggregates to surrounding cells, promoting pathology via poorly understood mechanisms. ... ...

    Abstract In human neurodegenerative diseases, neurons can transfer toxic protein aggregates to surrounding cells, promoting pathology via poorly understood mechanisms. In
    MeSH term(s) Animals ; Caenorhabditis elegans/metabolism ; Caenorhabditis elegans Proteins/metabolism ; Epidermal Growth Factor/metabolism ; Fibroblast Growth Factors/metabolism ; Genes, ras/genetics ; Lipogenesis/physiology ; MAP Kinase Signaling System/physiology ; Neurodegenerative Diseases/metabolism ; Neurons/metabolism ; Oxidation-Reduction ; Signal Transduction ; Stress, Physiological/physiology
    Chemical Substances Caenorhabditis elegans Proteins ; Fibroblast Growth Factors (62031-54-3) ; Epidermal Growth Factor (62229-50-9)
    Language English
    Publishing date 2021-08-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2101410118
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    Zs.A 1148: Show issues Location:
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