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  1. Artikel ; Online: Fast-evolving cofactors regulate the role of HEATR5 complexes in intra-Golgi trafficking.

    Marmorale, Lucas J / Jin, Huan / Reidy, Thomas G / Palomino-Alonso, Brandon / Zysnarski, Christopher J / Jordan-Javed, Fatima / Lahiri, Sagar / Duncan, Mara C

    The Journal of cell biology

    2024  Band 223, Heft 3

    Abstract: The highly conserved HEATR5 proteins are best known for their roles in membrane traffic mediated by the adaptor protein complex-1 (AP1). HEATR5 proteins rely on fast-evolving cofactors to bind to AP1. However, how HEATR5 proteins interact with these ... ...

    Abstract The highly conserved HEATR5 proteins are best known for their roles in membrane traffic mediated by the adaptor protein complex-1 (AP1). HEATR5 proteins rely on fast-evolving cofactors to bind to AP1. However, how HEATR5 proteins interact with these cofactors is unknown. Here, we report that the budding yeast HEATR5 protein, Laa1, functions in two biochemically distinct complexes. These complexes are defined by a pair of mutually exclusive Laa1-binding proteins, Laa2 and the previously uncharacterized Lft1/Yml037c. Despite limited sequence similarity, biochemical analysis and structure predictions indicate that Lft1 and Laa2 bind Laa1 via structurally similar mechanisms. Both Laa1 complexes function in intra-Golgi recycling. However, only the Laa2-Laa1 complex binds to AP1 and contributes to its localization. Finally, structure predictions indicate that human HEATR5 proteins bind to a pair of fast-evolving interacting partners via a mechanism similar to that observed in yeast. These results reveal mechanistic insight into how HEATR5 proteins bind their cofactors and indicate that Laa1 performs functions besides recruiting AP1.
    Mesh-Begriff(e) Humans ; Adaptor Protein Complex 1/metabolism ; Carrier Proteins/metabolism ; Golgi Apparatus/metabolism ; Saccharomyces cerevisiae/metabolism ; Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemische Substanzen Adaptor Protein Complex 1 ; Carrier Proteins ; HEATR5B protein, human ; Laa1 protein, S cerevisiae ; Adaptor Proteins, Signal Transducing ; Saccharomyces cerevisiae Proteins
    Sprache Englisch
    Erscheinungsdatum 2024-01-19
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202309047
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel: Two functionally distinct HEATR5 protein complexes are defined by fast-evolving co-factors in yeast.

    Marmorale, Lucas J / Jin, Huan / Reidy, Thomas G / Palomino-Alonso, Brandon / Zysnarski, Christopher / Jordan-Javed, Fatima / Lahiri, Sagar / Duncan, Mara C

    bioRxiv : the preprint server for biology

    2023  

    Abstract: The highly conserved HEATR5 proteins are best known for their roles in membrane traffic mediated by the adaptor protein complex-1 (AP1). HEATR5 proteins rely on fast-evolving co-factors to bind to AP1. However, how HEATR5 proteins interact with these co- ... ...

    Abstract The highly conserved HEATR5 proteins are best known for their roles in membrane traffic mediated by the adaptor protein complex-1 (AP1). HEATR5 proteins rely on fast-evolving co-factors to bind to AP1. However, how HEATR5 proteins interact with these co-factors is unknown. Here, we report that the budding yeast HEATR5 protein, Laa1, functions in two biochemically distinct complexes. These complexes are defined by a pair of mutually exclusive Laa1-binding proteins, Laa2 and the previously uncharacterized Lft1/Yml037c. Despite limited sequence similarity, biochemical analysis and structure predictions indicate that Lft1 and Laa2 bind Laa1 via structurally similar mechanisms. Both Laa1 complexes function in intra-Golgi recycling. However, only the Laa2-Laa1 complex binds to AP1 and contributes to its localization. Finally, structure predictions indicate that human HEATR5 proteins bind to a pair of fast-evolving interacting partners via a mechanism similar to that observed in yeast. These results reveal mechanistic insight into how HEATR5 proteins bind their co-factors and indicate that Laa1 performs functions besides recruiting AP1.
    Sprache Englisch
    Erscheinungsdatum 2023-11-27
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2023.08.24.554671
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Adaptor protein complex-1 (AP-1) is recruited by the HEATR5 protein Laa1 and its co-factor Laa2 in yeast.

    Zysnarski, Christopher J / Lahiri, Sagar / Javed, Fatima T / Martínez-Márquez, Jorge Y / Trowbridge, Justin W / Duncan, Mara C

    The Journal of biological chemistry

    2018  Band 294, Heft 4, Seite(n) 1410–1419

    Abstract: Cellular membrane trafficking mediated by the clathrin adaptor protein complex-1 (AP-1) is important for the proper composition and function of organelles of the endolysosomal system. Normal AP-1 function requires proteins of the HEAT repeat-containing 5 ...

    Abstract Cellular membrane trafficking mediated by the clathrin adaptor protein complex-1 (AP-1) is important for the proper composition and function of organelles of the endolysosomal system. Normal AP-1 function requires proteins of the HEAT repeat-containing 5 (HEATR5) family. Although HEATR5 proteins were first identified based on their ability to interact with AP-1, the functional significance of this interaction was unknown. We used bioinformatics-based phenotypic profiling and information from genome-wide fluorescence microscopy studies in the budding yeast
    Mesh-Begriff(e) Adaptor Protein Complex 1/chemistry ; Adaptor Protein Complex 1/metabolism ; Adaptor Proteins, Signal Transducing/chemistry ; Adaptor Proteins, Signal Transducing/metabolism ; Computational Biology ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; Microscopy, Fluorescence ; Phenotype ; Saccharomyces cerevisiae/chemistry ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism
    Chemische Substanzen Adaptor Protein Complex 1 ; Adaptor Proteins, Signal Transducing ; DNA-Binding Proteins ; Laa1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; YBL010C protein, S cerevisiae
    Sprache Englisch
    Erscheinungsdatum 2018-12-06
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.RA118.005253
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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