LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Your last searches

  1. AU="Larus, Isabel"
  2. AU="Wilkinson, Darren J"
  3. AU="Phil Bronstein"
  4. AU="Johnston, C"

Search results

Result 1 - 3 of total 3

Search options

  1. Article: C. elegans

    DeGroot, Melisa S / Williams, Byron / Chang, Timothy Y / Maas Gamboa, Maria L / Larus, Isabel / Fromme, J Christopher / Liu, Jun

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Secreted modular calcium binding (SMOC) proteins are conserved matricellular proteins found in organisms ... ...

    Abstract Secreted modular calcium binding (SMOC) proteins are conserved matricellular proteins found in organisms from
    Language English
    Publishing date 2023-01-08
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.01.06.523017
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  2. Article ; Online: SMOC-1 interacts with both BMP and glypican to regulate BMP signaling in C. elegans.

    DeGroot, Melisa S / Williams, Byron / Chang, Timothy Y / Maas Gamboa, Maria L / Larus, Isabel M / Hong, Garam / Fromme, J Christopher / Liu, Jun

    PLoS biology

    2023  Volume 21, Issue 8, Page(s) e3002272

    Abstract: Secreted modular calcium-binding proteins (SMOCs) are conserved matricellular proteins found in organisms from Caenorhabditis elegans to humans. SMOC homologs characteristically contain 1 or 2 extracellular calcium-binding (EC) domain(s) and 1 or 2 ... ...

    Abstract Secreted modular calcium-binding proteins (SMOCs) are conserved matricellular proteins found in organisms from Caenorhabditis elegans to humans. SMOC homologs characteristically contain 1 or 2 extracellular calcium-binding (EC) domain(s) and 1 or 2 thyroglobulin type-1 (TY) domain(s). SMOC proteins in Drosophila and Xenopus have been found to interact with cell surface heparan sulfate proteoglycans (HSPGs) to exert both positive and negative influences on the conserved bone morphogenetic protein (BMP) signaling pathway. In this study, we used a combination of biochemical, structural modeling, and molecular genetic approaches to dissect the functions of the sole SMOC protein in C. elegans. We showed that CeSMOC-1 binds to the heparin sulfate proteoglycan GPC3 homolog LON-2/glypican, as well as the mature domain of the BMP2/4 homolog DBL-1. Moreover, CeSMOC-1 can simultaneously bind LON-2/glypican and DBL-1/BMP. The interaction between CeSMOC-1 and LON-2/glypican is mediated specifically by the EC domain of CeSMOC-1, while the full interaction between CeSMOC-1 and DBL-1/BMP requires full-length CeSMOC-1. We provide both in vitro biochemical and in vivo functional evidence demonstrating that CeSMOC-1 functions both negatively in a LON-2/glypican-dependent manner and positively in a DBL-1/BMP-dependent manner to regulate BMP signaling. We further showed that in silico, Drosophila and vertebrate SMOC proteins can also bind to mature BMP dimers. Our work provides a mechanistic basis for how the evolutionarily conserved SMOC proteins regulate BMP signaling.
    MeSH term(s) Animals ; Biological Transport ; Caenorhabditis elegans ; Caenorhabditis elegans Proteins/metabolism ; Glypicans/metabolism ; Signal Transduction ; Bone Morphogenetic Proteins/metabolism ; Calcium-Binding Proteins/metabolism
    Chemical Substances Caenorhabditis elegans Proteins ; Glypicans ; LON-2 protein, C elegans ; Bone Morphogenetic Proteins ; Smoc-1 protein, C elegans ; Calcium-Binding Proteins
    Language English
    Publishing date 2023-08-17
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2126776-5
    ISSN 1545-7885 ; 1544-9173
    ISSN (online) 1545-7885
    ISSN 1544-9173
    DOI 10.1371/journal.pbio.3002272
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

  3. Article: Effects of Signal Disruption Depends on the Substrate Preference of the Lactonase.

    Mahan, Kathleen / Martinmaki, Ryan / Larus, Isabel / Sikdar, Rakesh / Dunitz, Jordan / Elias, Mikael

    Frontiers in microbiology

    2020  Volume 10, Page(s) 3003

    Abstract: Many bacteria produce and use extracellular signaling molecules such as acyl homoserine lactones (AHLs) to communicate and coordinate behavior in a cell-density dependent manner, ...

    Abstract Many bacteria produce and use extracellular signaling molecules such as acyl homoserine lactones (AHLs) to communicate and coordinate behavior in a cell-density dependent manner,
    Language English
    Publishing date 2020-01-14
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2019.03003
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

To top