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  1. Article ; Online: Acylation – A New Means to Control Traffic Through the Golgi

    Andreas M. Ernst / Derek Toomre / Jonathan S. Bogan

    Frontiers in Cell and Developmental Biology, Vol

    2019  Volume 7

    Abstract: The Golgi is well known to act as center for modification and sorting of proteins for secretion and delivery to other organelles. A key sorting step occurs at the trans-Golgi network and is mediated by protein adapters. However, recent data indicate that ...

    Abstract The Golgi is well known to act as center for modification and sorting of proteins for secretion and delivery to other organelles. A key sorting step occurs at the trans-Golgi network and is mediated by protein adapters. However, recent data indicate that sorting also occurs much earlier, at the cis-Golgi, and uses lipid acylation as a novel means to regulate anterograde flux. Here, we examine an emerging role of S-palmitoylation/acylation as a mechanism to regulate anterograde routing. We discuss the critical Golgi-localized DHHC S-palmitoyltransferase enzymes that orchestrate this lipid modification, as well as their diverse protein clients (e.g., MAP6, SNAP25, CSP, LAT, β-adrenergic receptors, GABA receptors, and GLUT4 glucose transporters). Critically, for integral membrane proteins, S-acylation can act as new a “self-sorting” signal to concentrate these cargoes in rims of Golgi cisternae, and to promote their rapid traffic through the Golgi or, potentially, to bypass the Golgi. We discuss this mechanism and examine its potential relevance to human physiology and disease, including diabetes and neurodegenerative diseases.
    Keywords Golgi ; palmitoylation ; acylation ; anterograde transport ; Golgi bypass ; membrane traffic ; Biology (General) ; QH301-705.5
    Subject code 571
    Language English
    Publishing date 2019-06-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: The intracellular helical bundle of human glucose transporter GLUT4 is important for complex formation with ASPL

    Peng Huang / Hannah Åbacka / Daniel Varela / Raminta Venskutonytė / Lotta Happonen / Jonathan S. Bogan / Pontus Gourdon / Mahmood R. Amiry‐Moghaddam / Ingmar André / Karin Lindkvist‐Petersson

    FEBS Open Bio, Vol 13, Iss 11, Pp 2094-

    2023  Volume 2107

    Abstract: Glucose transporters (GLUTs) are responsible for transporting hexose molecules across cellular membranes. In adipocytes, insulin stimulates glucose uptake by redistributing GLUT4 to the plasma membrane. In unstimulated adipose‐like mouse cell lines, ... ...

    Abstract Glucose transporters (GLUTs) are responsible for transporting hexose molecules across cellular membranes. In adipocytes, insulin stimulates glucose uptake by redistributing GLUT4 to the plasma membrane. In unstimulated adipose‐like mouse cell lines, GLUT4 is known to be retained intracellularly by binding to TUG protein, while upon insulin stimulation, GLUT4 dissociates from TUG. Here, we report that the TUG homolog in human, ASPL, exerts similar properties, i.e., forms a complex with GLUT4. We describe the structural details of complex formation by combining biochemical assays with cross‐linking mass spectrometry and computational modeling. Combined, the data suggest that the intracellular domain of GLUT4 binds to the helical lariat of ASPL and contributes to the regulation of GLUT4 trafficking by cooperative binding.
    Keywords adipocyte ; ASPL ; glucose transporters ; GLUT4 ; trafficking ; TUG ; Biology (General) ; QH301-705.5
    Subject code 571
    Language English
    Publishing date 2023-11-01T00:00:00Z
    Publisher Wiley
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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