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  1. Article ; Online: A cornichon protein controls polar localization of the PINA auxin transporter in Physcomitrium patens.

    Yáñez-Domínguez, Carolina / Lagunas-Gómez, Daniel / Torres-Cifuentes, Diana M / Bezanilla, Magdalena / Pantoja, Omar

    Development (Cambridge, England)

    2023  Volume 150, Issue 9

    Abstract: Newly synthesized membrane proteins pass through the secretory pathway, starting at the endoplasmic reticulum and packaged into COPII vesicles, to continue to the Golgi apparatus before reaching their membrane of residence. It is known that cargo ... ...

    Abstract Newly synthesized membrane proteins pass through the secretory pathway, starting at the endoplasmic reticulum and packaged into COPII vesicles, to continue to the Golgi apparatus before reaching their membrane of residence. It is known that cargo receptor proteins form part of the COPII complex and play a role in the recruitment of cargo proteins for their subsequent transport through the secretory pathway. The role of cornichon proteins is conserved from yeast to vertebrates, but it is poorly characterized in plants. Here, we studied the role of the two cornichon homologs in the secretory pathway of the moss Physcomitrium patens. Mutant analyses revealed that cornichon genes regulate different growth processes during the moss life cycle by controlling auxin transport, with CNIH2 functioning as a specific cargo receptor for the auxin efflux carrier PINA, with the C terminus of the receptor regulating the interaction, trafficking and membrane localization of PINA.
    MeSH term(s) Animals ; Protein Transport ; COP-Coated Vesicles/metabolism ; Membrane Transport Proteins/metabolism ; Biological Transport/physiology ; Membrane Proteins/metabolism ; Carrier Proteins/metabolism ; Golgi Apparatus/metabolism ; Saccharomyces cerevisiae/metabolism
    Chemical Substances Membrane Transport Proteins ; Membrane Proteins ; Carrier Proteins
    Language English
    Publishing date 2023-05-05
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 90607-4
    ISSN 1477-9129 ; 0950-1991
    ISSN (online) 1477-9129
    ISSN 0950-1991
    DOI 10.1242/dev.201635
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ub I Zs.183: Show issues Location:
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  2. Article ; Online: The C-terminus of the cargo receptor Erv14 affects COPII vesicle formation and cargo delivery.

    Lagunas-Gomez, Daniel / Yañez-Dominguez, Carolina / Zavala-Padilla, Guadalupe / Barlowe, Charles / Pantoja, Omar

    Journal of cell science

    2023  Volume 136, Issue 3

    Abstract: The endoplasmic reticulum (ER) is the start site of the secretory pathway, where newly synthesized secreted and membrane proteins are packaged into COPII vesicles through direct interaction with the COPII coat or aided by specific cargo receptors. Little ...

    Abstract The endoplasmic reticulum (ER) is the start site of the secretory pathway, where newly synthesized secreted and membrane proteins are packaged into COPII vesicles through direct interaction with the COPII coat or aided by specific cargo receptors. Little is known about how post-translational modification events regulate packaging of cargo into COPII vesicles. The Saccharomyces cerevisiae protein Erv14, also known as cornichon, belongs to a conserved family of cargo receptors required for the selection and ER export of transmembrane proteins. In this work, we show the importance of a phosphorylation consensus site (S134) at the C-terminus of Erv14. Mimicking phosphorylation of S134 (S134D) prevents the incorporation of Erv14 into COPII vesicles, delays cell growth, exacerbates growth of sec mutants, modifies ER structure and affects localization of several plasma membrane transporters. In contrast, the dephosphorylated mimic (S134A) had less deleterious effects, but still modifies ER structure and slows cell growth. Our results suggest that a possible cycle of phosphorylation and dephosphorylation is important for the correct functioning of Erv14.
    MeSH term(s) Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Membrane Proteins/metabolism ; Carrier Proteins/metabolism ; Membrane Transport Proteins/metabolism ; Biological Transport ; COP-Coated Vesicles/metabolism ; Protein Transport
    Chemical Substances Saccharomyces cerevisiae Proteins ; Membrane Proteins ; Carrier Proteins ; Membrane Transport Proteins
    Language English
    Publishing date 2023-02-06
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.260527
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  3. Article: Plant and yeast cornichon possess a conserved acidic motif required for correct targeting of plasma membrane cargos.

    Rosas-Santiago, Paul / Lagunas-Gomez, Daniel / Yáñez-Domínguez, Carolina / Vera-Estrella, Rosario / Zimmermannová, Olga / Sychrová, Hana / Pantoja, Omar

    Biochimica et biophysica acta. Molecular cell research

    2017  Volume 1864, Issue 10, Page(s) 1809–1818

    Abstract: The export of membrane proteins along the secretory pathway is initiated at the endoplasmic reticulum after proteins are folded and packaged inside this organelle by their recruiting into the coat complex COPII vesicles. It is proposed that cargo ... ...

    Abstract The export of membrane proteins along the secretory pathway is initiated at the endoplasmic reticulum after proteins are folded and packaged inside this organelle by their recruiting into the coat complex COPII vesicles. It is proposed that cargo receptors are required for the correct transport of proteins to its target membrane, however, little is known about ER export signals for cargo receptors. Erv14/Cornichon belong to a well conserved protein family in Eukaryotes, and have been proposed to function as cargo receptors for many transmembrane proteins. Amino acid sequence alignment showed the presence of a conserved acidic motif in the C-terminal in homologues from plants and yeast. Here, we demonstrate that mutation of the C-terminal acidic motif from ScErv14 or OsCNIH1, did not alter the localization of these cargo receptors, however it modified the proper targeting of the plasma membrane transporters Nha1p, Pdr12p and Qdr2p. Our results suggest that mistargeting of these plasma membrane proteins is a consequence of a weaker interaction between the cargo receptor and cargo proteins caused by the mutation of the C-terminal acidic motif.
    MeSH term(s) ATP-Binding Cassette Transporters/genetics ; Amino Acid Motifs/genetics ; Amino Acid Sequence/genetics ; COP-Coated Vesicles/genetics ; COP-Coated Vesicles/metabolism ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Endoplasmic Reticulum/genetics ; Endoplasmic Reticulum/metabolism ; Golgi Apparatus/genetics ; Golgi Apparatus/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Membrane Transport Proteins/genetics ; Oryza/genetics ; Protein Folding ; Protein Transport/genetics ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics ; Sequence Alignment ; Sodium-Hydrogen Exchangers/genetics
    Chemical Substances ATP-Binding Cassette Transporters ; Erv14 protein, S cerevisiae ; Membrane Proteins ; Membrane Transport Proteins ; NHX1 protein, S cerevisiae ; Pdr12 protein, S cerevisiae ; Qdr2 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Sodium-Hydrogen Exchangers
    Language English
    Publishing date 2017-07-16
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0167-4889 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0167-4889 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamcr.2017.07.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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