An electron microscopic study of TGN38/41 dynamics

Ladinsky, Mark S.; Howell, Kathryn E.

doi:10.1242/jcs.1993.supplement_17.7

Cited by 20 publications

(9 citation statements)

References 16 publications

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“…In order to retain good morphology for comparing results obtained by deconvolution microscopy and cryoIEM of tissue sections, we utilized the R3195 polyclonal antibody. Moreover, given the difficulty in detecting VTCs containing p58 or Syn5 in tissues (due to the compactness of cells in tissue sections), we examined the distribution of CFTR relative to the distribution of TGN38 [45,61], and α‐mannosidase I (10E6), a cis Golgi network (CGN) marker [62].…”

Section: Resultsmentioning

confidence: 99%

Traffic Pattern of Cystic Fibrosis Transmembrane Regulator through the Early Exocytic Pathway

Bannykh

Fish

et al. 2000

Traffic

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The pathway of transport of the cystic fibrosis transmembrane regulator (CFTR) through the early exocytic pathway has not been examined. In contrast to most membrane proteins that are concentrated during export from the ER and therefore readily detectable at elevated levels in pre-Golgi intermediates and Golgi compartments, wild-type CFTR could not be detected in these compartments using deconvolution immunofluorescence microscopy. To determine the basis for this unusual feature, we analyzed CFTR localization using quantitative immunoelectron microscopy (IEM). We found that wild-type CFTR is present in pre-Golgi compartments and peripheral tubular elements associated with the cis and trans faces of the Golgi stack, albeit at a concentration 2-fold lower than that found in the endoplasmic reticulum (ER). DF508 CFTR, a mutant form that is not efficiently delivered to the cell surface and the most common mutation in cystic fibrosis, could also be detected at a reduced concentration in pre-Golgi intermediates and peripheral cis Golgi elements, but not in post-Golgi compartments. Our results suggest that the low level of wild-type CFTR in the Golgi region reflects a limiting step in selective recruitment by the ER export machinery, an event that is largely deficient in DF508. We raise the possibility that novel modes of selective anterograde and retrograde traffic between the ER and the Golgi may serve to regulate CFTR function in the early secretory compartments.

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Section: Resultsmentioning

confidence: 99%

Traffic Pattern of Cystic Fibrosis Transmembrane Regulator through the Early Exocytic Pathway

Bannykh

Fish

et al. 2000

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“…Among the populations of secretory vesicles budding from the TGN, there are distinct vesicles that have been defined by their content proteins or by their inherent membrane proteins (10,(31)(32)(33). Due to the overlapping distribution of TGN38, it will be of interest to determine whether p200 is present on the specific population of exocytic vesicles demarked by TGN38 (32). A proportion of the budded, coated vesicles in intact cells and in Golgi membrane pellets were consistently unlabeled with p200 or 1-COP antibodies, suggesting the presence of yet other vesicle populations.…”

Section: Discussionmentioning

confidence: 99%

Distinct coated vesicles labeled for p200 bud from trans-Golgi network membranes.

Narula

Stow

1995

Proc. Natl. Acad. Sci. U.S.A.

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Golgi-associated cytoplasmic proteins, such as the coatomer protein complex, are required for vesicle budding and trafficking. We have previously described a cytoplasmic phosphoprotein, p200, which binds dynamically and specifically to Golgi membranes. The p200 protein is dissociated from Golgi membranes in the presence of brefeldin A and it is induced to bind to Golgi membranes by activation of guanine nucleotide binding proteins (G proteins) with guanosine 5'-[gamma-thio]triphosphate or aluminum fluoride. To establish the role of p200 in vesicle budding, we localized membrane-bound p200 in intact cells and on isolated Golgi membranes. We show that p200 is preferentially associated with vesicles in the trans-Golgi network (TGN). Activation of G proteins induced budding and accumulation of small, coated vesicles from Golgi membranes and p200 was localized on the cytoplasmic surface of some of these vesicles. Using immunogold labeling we further demonstrate that p200 and beta-COP are localized on different populations of Golgi-derived vesicles. These data establish that p200 is involved in the budding and coating of a class of Goli vesicles that are likely to be derived from the TGN. The data also show that there are distinct populations of non-clathrin-coated vesicles budded from Golgi membranes, and vesicles labeled for either beta-COP or p200 may represent transport vesicles for separate steps of protein transport.

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“…Depletion of ARF1 and ARF3 does not affect retrograde transport from endosomes to the Golgi complex or lysosomal transport Rat TGN38 and its human orthologue, TGN46, cycle between the plasma membrane and the TGN at a very low rate (Ladinsky and Howell, 1993;Reaves et al, 1993), although at steady state these proteins localize mainly to the TGN. During retrograde transport from the plasma membrane to the TGN, TGN38/TGN46 passes through early/recycling endosomes (Ghosh et al, 1998;Mallet and Maxfield, 1999;Maxfield and McGraw, 2004).…”

Section: Endosomal Tubulation Cannot Be Rescued By the Arf1(n52r) Mutantmentioning

confidence: 97%

ARF1 and ARF3 Are Required for the Integrity of Recycling Endosomes and the Recycling Pathway

Kondo

Hanai

Nakai

et al. 2012

Cell Struct. Funct.

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ABSTRACT. Small GTPases ARF1 and ARF3 localize mainly to the Golgi apparatus, where they trigger formation of coated carrier vesicles. We previously showed that BIG2, a guanine nucleotide exchange factor specific for ARF1 and ARF3, localizes not only to the trans-Golgi network (TGN) but also to recycling endosomes, where it is involved in regulating the integrity of recycling endosomes. However, it is not yet clear whether ARF1 and ARF3 act downstream of BIG2 to ensure endosome integrity. In this study, we show that EGFP-tagged ARF1 and ARF3 localize to endosomal compartments containing endocytosed transferrin. We further demonstrate that simultaneous depletion of ARF1 and ARF3 induces tubulation of recycling endosomal compartments positive for transferrin receptor, Rab4, and Rab11, but does not significantly affect the integrity of the Golgi apparatus or early or late endosomes. Moreover, the simultaneous depletion of ARF1 and ARF3 suppresses recycling of transferrin but does not affect either its endocytosis or the retrograde transport of TGN38 from early/recycling endosomes to the TGN. In addition, depletion of ARF1 and ARF3 does not affect retrograde transport of CD4-furin from late endosomes to the TGN, or of endocytosed EGF from late endosomes to lysosomes. These results indicate that ARF1 and ARF3 are redundantly required for the integrity of recycling endosomes, and that they regulate transferrin recycling from endosomes to the plasma membrane, but not retrograde transport from endosomal compartments to the TGN.

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An electron microscopic study of TGN38/41 dynamics

Cited by 20 publications

References 16 publications

Traffic Pattern of Cystic Fibrosis Transmembrane Regulator through the Early Exocytic Pathway

Traffic Pattern of Cystic Fibrosis Transmembrane Regulator through the Early Exocytic Pathway

Distinct coated vesicles labeled for p200 bud from trans-Golgi network membranes.

ARF1 and ARF3 Are Required for the Integrity of Recycling Endosomes and the Recycling Pathway

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