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  1. Article ; Online: Waxy lipids and waning insulin secretion.

    Bogan, Jonathan S

    Nature cell biology

    2022  Volume 25, Issue 1, Page(s) 7–8

    MeSH term(s) Waxes ; Insulin Secretion ; Blood Glucose ; Insulin/metabolism
    Chemical Substances Waxes ; Blood Glucose ; Insulin
    Language English
    Publishing date 2022-12-21
    Publishing country England
    Document type Journal Article
    ZDB-ID 1474722-4
    ISSN 1476-4679 ; 1465-7392
    ISSN (online) 1476-4679
    ISSN 1465-7392
    DOI 10.1038/s41556-022-01036-1
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  2. Article: Ubiquitin-like processing of TUG proteins as a mechanism to regulate glucose uptake and energy metabolism in fat and muscle.

    Bogan, Jonathan S

    Frontiers in endocrinology

    2022  Volume 13, Page(s) 1019405

    Abstract: In response to insulin stimulation, fat and muscle cells mobilize GLUT4 glucose transporters to the cell surface to enhance glucose uptake. Ubiquitin-like processing of TUG (Aspscr1, UBXD9) proteins is a central mechanism to regulate this process. Here, ... ...

    Abstract In response to insulin stimulation, fat and muscle cells mobilize GLUT4 glucose transporters to the cell surface to enhance glucose uptake. Ubiquitin-like processing of TUG (Aspscr1, UBXD9) proteins is a central mechanism to regulate this process. Here, recent advances in this area are reviewed. The data support a model in which intact TUG traps insulin-responsive "GLUT4 storage vesicles" at the Golgi matrix by binding vesicle cargoes with its N-terminus and matrix proteins with its C-terminus. Insulin stimulation liberates these vesicles by triggering endoproteolytic cleavage of TUG, mediated by the Usp25m protease. Cleavage occurs in fat and muscle cells, but not in fibroblasts or other cell types. Proteolytic processing of intact TUG generates TUGUL, a ubiquitin-like protein modifier, as the N-terminal cleavage product. In adipocytes, TUGUL modifies a single protein, the KIF5B kinesin motor, which carries GLUT4 and other vesicle cargoes to the cell surface. In muscle, this or another motor may be modified. After cleavage of intact TUG, the TUG C-terminal product is extracted from the Golgi matrix by the p97 (VCP) ATPase. In both muscle and fat, this cleavage product enters the nucleus, binds PPARγ and PGC-1α, and regulates gene expression to promote fatty acid oxidation and thermogenesis. The stability of the TUG C-terminal product is regulated by an Ate1 arginyltransferase-dependent N-degron pathway, which may create a feedback mechanism to control oxidative metabolism. Although it is now clear that TUG processing coordinates glucose uptake with other aspects of physiology and metabolism, many questions remain about how this pathway is regulated and how it is altered in metabolic disease in humans.
    MeSH term(s) Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Energy Metabolism ; Fatty Acids/metabolism ; Glucose/metabolism ; Humans ; Insulin/metabolism ; Intracellular Signaling Peptides and Proteins/metabolism ; Kinesins ; Muscles ; PPAR gamma/metabolism ; Peptide Hydrolases/metabolism ; Protein Transport ; Ubiquitin/metabolism
    Chemical Substances ASPSCR1 protein, human ; Carrier Proteins ; Fatty Acids ; Insulin ; Intracellular Signaling Peptides and Proteins ; PPAR gamma ; Ubiquitin ; Peptide Hydrolases (EC 3.4.-) ; Kinesins (EC 3.6.4.4) ; Glucose (IY9XDZ35W2)
    Language English
    Publishing date 2022-09-29
    Publishing country Switzerland
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ZDB-ID 2592084-4
    ISSN 1664-2392
    ISSN 1664-2392
    DOI 10.3389/fendo.2022.1019405
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  3. Article ; Online: Granular detail of β cell structures for insulin secretion.

    Bogan, Jonathan S

    The Journal of cell biology

    2021  Volume 220, Issue 2

    Abstract: Pancreatic β cells secrete insulin in response to increased glucose concentrations. Müller et al. (2021. J. Cell Biol. https://doi.org/10.1083/jcb.202010039) use 3D FIB-SEM to study the architecture of these cells and to elucidate how glucose stimulation ...

    Abstract Pancreatic β cells secrete insulin in response to increased glucose concentrations. Müller et al. (2021. J. Cell Biol. https://doi.org/10.1083/jcb.202010039) use 3D FIB-SEM to study the architecture of these cells and to elucidate how glucose stimulation remodels microtubules to control insulin secretory granule exocytosis.
    MeSH term(s) Exocytosis ; Insulin/metabolism ; Insulin Secretion ; Insulin-Secreting Cells/metabolism ; Secretory Vesicles/metabolism
    Chemical Substances Insulin
    Language English
    Publishing date 2021-01-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202012082
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  4. Article ; Online: Diabetes and COVID-19, a link revealed.

    Xiao, Xiaoping / Tong, Liangqin / Bogan, Jonathan S / Wang, Penghua / Cheng, Gong

    Life medicine

    2022  Volume 1, Issue 2, Page(s) 64–66

    Language English
    Publishing date 2022-06-28
    Publishing country England
    Document type Journal Article
    ISSN 2755-1733
    ISSN (online) 2755-1733
    DOI 10.1093/lifemedi/lnac011
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  5. Article ; Online: Endocytic cycling of glucose transporters and insulin resistance due to immunosuppressive agents.

    Bogan, Jonathan S

    The Journal of clinical endocrinology and metabolism

    2014  Volume 99, Issue 10, Page(s) 3622–3624

    MeSH term(s) Adipocytes/drug effects ; Cyclosporine/pharmacology ; Endocytosis/drug effects ; Female ; Glucose Transporter Type 4/metabolism ; Humans ; Male ; Prediabetic State/chemically induced ; Tacrolimus/pharmacology
    Chemical Substances Glucose Transporter Type 4 ; SLC2A4 protein, human ; Cyclosporine (83HN0GTJ6D) ; Tacrolimus (WM0HAQ4WNM)
    Language English
    Publishing date 2014-10-03
    Publishing country United States
    Document type Editorial ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 3029-6
    ISSN 1945-7197 ; 0021-972X
    ISSN (online) 1945-7197
    ISSN 0021-972X
    DOI 10.1210/jc.2014-3305
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  6. Article: Acylation - A New Means to Control Traffic Through the Golgi.

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

    Frontiers in cell and developmental biology

    2019  Volume 7, Page(s) 109

    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 ... ...

    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
    Language English
    Publishing date 2019-06-12
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2019.00109
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  7. Article ; Online: Regulation of glucose transporter translocation in health and diabetes.

    Bogan, Jonathan S

    Annual review of biochemistry

    2012  Volume 81, Page(s) 507–532

    Abstract: To enhance glucose uptake into muscle and fat cells, insulin stimulates the translocation of GLUT4 glucose transporters from intracellular membranes to the cell surface. This response requires the intersection of insulin signaling and vesicle trafficking ...

    Abstract To enhance glucose uptake into muscle and fat cells, insulin stimulates the translocation of GLUT4 glucose transporters from intracellular membranes to the cell surface. This response requires the intersection of insulin signaling and vesicle trafficking pathways, and it is compromised in the setting of overnutrition to cause insulin resistance. Insulin signals through AS160/Tbc1D4 and Tbc1D1 to modulate Rab GTPases and through the Rho GTPase TC10α to act on other targets. In unstimulated cells, GLUT4 is incorporated into specialized storage vesicles containing IRAP, LRP1, sortilin, and VAMP2, which are sequestered by TUG, Ubc9, and other proteins. Insulin mobilizes these vesicles directly to the plasma membrane, and it modulates the trafficking itinerary so that cargo recycles from endosomes during ongoing insulin exposure. Knowledge of how signaling and trafficking pathways are coordinated will be essential to understanding the pathogenesis of diabetes and the metabolic syndrome and may also inform a wide range of other physiologies.
    MeSH term(s) Animals ; Diabetes Mellitus/metabolism ; Glucose/metabolism ; Glucose Transport Proteins, Facilitative/metabolism ; Humans ; Insulin/metabolism ; Signal Transduction
    Chemical Substances Glucose Transport Proteins, Facilitative ; Insulin ; Glucose (IY9XDZ35W2)
    Language English
    Publishing date 2012-04-05
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 207924-0
    ISSN 1545-4509 ; 0066-4154
    ISSN (online) 1545-4509
    ISSN 0066-4154
    DOI 10.1146/annurev-biochem-060109-094246
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  8. Article: Vasopressin inactivation: Role of insulin-regulated aminopeptidase.

    Li, Don T / Habtemichael, Estifanos N / Bogan, Jonathan S

    Vitamins and hormones

    2019  Volume 113, Page(s) 101–128

    Abstract: The physiological importance of vasopressin inactivation has long been appreciated, but the mechanisms and potential pathophysiologic roles of this process remain active subjects of research. Human Placental Leucine Aminopeptidase (P-LAP, encoded by the ... ...

    Abstract The physiological importance of vasopressin inactivation has long been appreciated, but the mechanisms and potential pathophysiologic roles of this process remain active subjects of research. Human Placental Leucine Aminopeptidase (P-LAP, encoded by the LNPEP gene) is an important determinant of vasopressinase activity during pregnancy and is associated with gestational diabetes insipidus and preeclampsia. Insulin-Regulated Aminopeptidase (IRAP), the rodent homologue of P-LAP, is coregulated with the insulin-responsive glucose transporter, GLUT4, in adipose and muscle cells. Recently, the Tether containing a UBX domain for GLUT4 (TUG) protein was shown to mediate the coordinated regulation of water and glucose homeostasis. TUG sequesters IRAP and GLUT4 intracellularly in the absence of insulin. Insulin and other stimuli cause the proteolytic cleavage of TUG to mobilize these proteins to the cell surface, where IRAP acts to terminate the activity of circulating vasopressin. Intriguingly, genetic variation in LNPEP is associated with the vasopressin response and mortality during sepsis, and increased copeptin, a marker of vasopressin secretion, is associated with cardiovascular and metabolic disease. We propose that in the setting of insulin resistance in muscle, increased cell-surface IRAP and accelerated vasopressin degradation cause a compensatory increase in vasopressin secretion. The increased vasopressin concentrations present at the kidneys then contribute to hypertension in the metabolic syndrome. Further analyses of metabolism and of vasopressin and copeptin may yield novel insights into a unified pathophysiologic mechanism linking insulin resistance and hypertension, and potentially other components of the metabolic syndrome, in humans.
    MeSH term(s) Aminopeptidases/metabolism ; Animals ; Humans ; Insulin/metabolism ; Models, Animal ; Rats ; Vasopressins/metabolism
    Chemical Substances Insulin ; Vasopressins (11000-17-2) ; Aminopeptidases (EC 3.4.11.-)
    Language English
    Publishing date 2019-10-18
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 201161-x
    ISSN 2162-2620 ; 0083-6729
    ISSN (online) 2162-2620
    ISSN 0083-6729
    DOI 10.1016/bs.vh.2019.08.017
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  9. 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: ... 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 ... receptors, and GLUT4 glucose transporters). Critically, for integral membrane proteins, S-acylation can act ...

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

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

    FEBS open bio

    2023  Volume 13, Issue 11, Page(s) 2094–2107

    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.
    MeSH term(s) Humans ; Mice ; Animals ; Carrier Proteins/metabolism ; Protein Transport ; Glucose/metabolism ; Glucose Transport Proteins, Facilitative/metabolism ; Intracellular Signaling Peptides and Proteins/metabolism ; Insulin/metabolism
    Chemical Substances Carrier Proteins ; Glucose (IY9XDZ35W2) ; Glucose Transport Proteins, Facilitative ; Intracellular Signaling Peptides and Proteins ; Insulin
    Language English
    Publishing date 2023-09-28
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2651702-4
    ISSN 2211-5463 ; 2211-5463
    ISSN (online) 2211-5463
    ISSN 2211-5463
    DOI 10.1002/2211-5463.13709
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