ArticleThe Journal of cell biology1997
Glucose transporter (GLUT-4) is targeted to secretory granules in rat atrial cardiomyocytes.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 76 citations in OpenAlex.
- Characterization of lipoprotein lipase storage vesicles in 3T3-L1 adipocytes.Journal of cell science · 2022Article
- Peptidylglycine α-amidating monooxygenase is required for atrial secretory granule formation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Mitochondrial PAK6 inhibits prostate cancer cell apoptosisTheranostics · 2020Article
- Development of a quantitative Correlative Light Electron Microscopy technique to study GLUT4 trafficking.Protoplasma · 2014Article
- Characterization of VAMP-2 in the lung: implication in lung surfactant secretion.Cell biology international · 2012Article
- Architecture of the mammalian Golgi.Cold Spring Harbor perspectives in biology · 2011Review
- VAMP-1, VAMP-2, and syntaxin-4 regulate ANP release from cardiac myocytes.Journal of molecular and cellular cardiology · 2010Article
- A common trafficking route for GLUT4 in cardiomyocytes in response to insulin, contraction and energy-status signalling.Journal of cell science · 2009Article
- Insulin-stimulated exocytosis of GLUT4 is enhanced by IRAP and its partner tankyrase.The Biochemical journal · 2007Article
- Not all secretory granules are created equal: Partitioning of soluble content proteins.Molecular biology of the cell · 2006Article
- Is there structural specificity in the reversible protein aggregates that are stored in secretory granules?Journal of molecular neuroscience : MN · 2004Review
- Syntaxin 6 regulates Glut4 trafficking in 3T3-L1 adipocytes.Molecular biology of the cell · 2003Article
- GLUT4 recycles via a trans-Golgi network (TGN) subdomain enriched in Syntaxins 6 and 16 but not TGN38: involvement of an acidic targeting motif.Molecular biology of the cell · 2003Article
- Insulin recruits GLUT4 from specialized VAMP2-carrying vesicles as well as from the dynamic endosomal/trans-Golgi network in rat adipocytes.Molecular biology of the cell · 2000Article
- Characterization of insulin-responsive GLUT4 storage vesicles isolated from 3T3-L1 adipocytes.Molecular and cellular biology · 2000Article
- Trafficking of Glut4-green fluorescent protein chimaeras in 3T3-L1 adipocytes suggests distinct internalization mechanisms regulating cell surface glut4 levels.The Biochemical journal · 1999Article
- Differential regulation of secretory compartments containing the insulin-responsive glucose transporter 4 in 3T3-L1 adipocytes.Molecular biology of the cell · 1999Article
- Two compartments for insulin-stimulated exocytosis in 3T3-L1 adipocytes defined by endogenous ACRP30 and GLUT4.The Journal of cell biology · 1999Article
- Analysis of GLUT4 distribution in whole skeletal muscle fibers: identification of distinct storage compartments that are recruited by insulin and muscle contractions.The Journal of cell biology · 1998Article
- Sorting and storage during secretory granule biogenesis: looking backward and looking forward.The Biochemical journal · 1998Review
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The insulin-responsive glucose transporter GLUT-4 is found in muscle and fat cells in the trans-Golgi reticulum (TGR) and in an intracellular tubulovesicular compartment, from where it undergoes insulin-dependent movement to the cell surface. To examine the relationship between these GLUT-4-containing compartments and the regulated secretory pathway we have localized GLUT-4 in atrial cardiomyocytes. This cell type secretes an antihypertensive hormone, referred to as the atrial natriuretic factor (ANF), in response to elevated blood pressure. We show that GLUT-4 is targeted in the atrial cell to the TGR and a tubulo-vesicular compartment, which is morphologically and functionally indistinguishable from the intracellular GLUT-4 compartment found in other types of myocytes and in fat cells, and in addition to the ANF secretory granules. Forming ANF granules are present throughout all Golgi cisternae but only become GLUT4 positive in the TGR. The inability of cyclohexamide treatment to effect the TGR localization of GLUT-4 indicates that GLUT-4 enters the ANF secretory granules at the TGR via the recycling pathway and not via the biosynthetic pathway. These data suggest that a large proportion of GLUT-4 must recycle via the TGR in insulin-sensitive cells. It will be important to determine if this is the pathway by which the insulin-regulatable tubulo-vesicular compartment is formed.
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