scholarly journals Epistatic Analysis of the Contribution of Rabs and Kifs to CATCHR Family Dependent Golgi Organization

2019 ◽  
Vol 7 ◽  
Author(s):  
Shijie Liu ◽  
Waqar Majeed ◽  
Pranas Grigaitis ◽  
Matthew J. Betts ◽  
Leslie K. Climer ◽  
...  
Keyword(s):  
Golgi Organization ◽  
Epistatic Analysis

scholarly journals Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis

2005 ◽  
Vol 169 (2) ◽  
pp. 285-295 ◽  
Author(s):  
Daniela A. Sahlender ◽  
Rhys C. Roberts ◽  
Susan D. Arden ◽  
Giulietta Spudich ◽  
Marcus J. Taylor ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Rna Interference ◽  
Vesicular Stomatitis Virus ◽  
Protein Interaction ◽  
Golgi Complex ◽  
Myosin Vi ◽  
Binding Partner ◽  
Binding Partners ◽  
Vesicular Stomatitis ◽  
Golgi Organization

Myosin VI plays a role in the maintenance of Golgi morphology and in exocytosis. In a yeast 2-hybrid screen we identified optineurin as a binding partner for myosin VI at the Golgi complex and confirmed this interaction in a range of protein interaction studies. Both proteins colocalize at the Golgi complex and in vesicles at the plasma membrane. When optineurin is depleted from cells using RNA interference, myosin VI is lost from the Golgi complex, the Golgi is fragmented and exocytosis of vesicular stomatitis virus G-protein to the plasma membrane is dramatically reduced. Two further binding partners for optineurin have been identified: huntingtin and Rab8. We show that myosin VI and Rab8 colocalize around the Golgi complex and in vesicles at the plasma membrane and overexpression of constitutively active Rab8-Q67L recruits myosin VI onto Rab8-positive structures. These results show that optineurin links myosin VI to the Golgi complex and plays a central role in Golgi ribbon formation and exocytosis.

scholarly journals Actin dynamics coupled to clathrin-coated vesicle formation at the trans-Golgi network

2004 ◽  
Vol 165 (6) ◽  
pp. 781-788 ◽  
Author(s):  
Sebastien Carreno ◽  
Åsa E. Engqvist-Goldstein ◽  
Claire X. Zhang ◽  
Kent L. McDonald ◽  
David G. Drubin
Keyword(s):  
Time Lapse ◽  
Actin Dynamics ◽  
Coated Vesicle ◽  
Cell Cortex ◽  
Actin Assembly ◽  
Trans Golgi Network ◽  
Lysosome Biogenesis ◽  
Diverse Species ◽  
Golgi Network ◽  
Golgi Organization

In diverse species, actin assembly facilitates clathrin-coated vesicle (CCV) formation during endocytosis. This role might be an adaptation specific to the unique environment at the cell cortex, or it might be fundamental, facilitating CCV formation on different membranes. Proteins of the Sla2p/Hip1R family bind to actin and clathrin at endocytic sites in yeast and mammals. We hypothesized that Hip1R might also coordinate actin assembly with clathrin budding at the trans-Golgi network (TGN). Using deconvolution and time-lapse microscopy, we showed that Hip1R is present on CCVs emerging from the TGN. These vesicles contain the mannose 6-phosphate receptor involved in targeting proteins to the lysosome, and the actin nucleating Arp2/3 complex. Silencing of Hip1R expression by RNAi resulted in disruption of Golgi organization and accumulation of F-actin structures associated with CCVs on the TGN. Hip1R silencing and actin poisons slowed cathepsin D exit from the TGN. These studies establish roles for Hip1R and actin in CCV budding from the TGN for lysosome biogenesis.

scholarly journals MIA3/TANGO1 enables efficient secretion by constraining COPII vesicle budding

2021 ◽  
Author(s):  
Janine McCaughey ◽  
Judith M. Mantell ◽  
Chris R. Neal ◽  
Kate Heesom ◽  
David J. Stephens
Keyword(s):  
Endoplasmic Reticulum ◽  
Light Microscopy ◽  
Secretory Pathway ◽  
Genome Engineering ◽  
High Volume ◽  
Vesicle Budding ◽  
Early Secretory Pathway ◽  
Copii Vesicle ◽  
Intermediate Compartment ◽  
Golgi Organization

AbstractComplex machinery is required to drive secretory cargo export from the endoplasmic reticulum. In vertebrates, this includes transport and Golgi organization protein 1 (TANGO1), encoded by the Mia3 gene. Here, using genome engineering of human cells light microscopy, secretion assays, and proteomics, we show loss of Mia3/TANGO1 results in formation of numerous vesicles and a loss of early secretory pathway integrity. This restricts secretion not only of large proteins like procollagens but of all types of secretory cargo. Our data shows that Mia3/TANGO1 constrains the propensity of COPII to form vesicles promoting instead the formation of the ER-Golgi intermediate compartment. Thus, Mia3/TANGO1 facilities the secretion of complex and high volume cargoes from vertebrate cells.

scholarly journals Cell-matrix adhesion controls Golgi organization and function by regulating Arf1 activation in anchorage dependent cells

2018 ◽  
Author(s):  
Vibha Singh ◽  
Chaitanya Erady ◽  
Nagaraj Balasubramanian
Keyword(s):  
Membrane Trafficking ◽  
Microtubule Network ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Summary Statement ◽  
Golgi Fragmentation ◽  
And Function ◽  
Golgi Organization ◽  
Cell Matrix Adhesion ◽  
Constitutively Active

AbstractCell-matrix adhesion regulates membrane trafficking to control anchorage-dependent signaling. While a dynamic Golgi complex can contribute to this pathway, its control by adhesion remains untested. We find the loss of adhesion rapidly disorganizes the Golgi in mouse and human fibroblast cells, its integrity restored rapidly on re-adhesion to fibronectin (but not poly-l-lysine coated beads) along the microtubule network. Adhesion regulates the trans-Golgi more prominently than the cis /cis-medial Golgi, though they show no fallback into the ER making this reorganization distinct from known Golgi fragmentation. This is controlled by an adhesion-dependent drop and recovery of Arf1 activation, mediated through the Arf1 GEF BIG1/2 over GBF1. Constitutively active Arf1 disrupts this regulation and prevents Golgi disorganization in non-adherent cells. Adhesion regulates active Arf1 binding to the microtubule minus-end motor protein dynein to control Golgi reorganization, which ciliobrevin blocks. This regulation by adhesion controls Golgi function, promoting cell surface glycosylation on the loss of adhesion that constitutively active Arf1 blocks. This study hence identifies cell-matrix adhesion to be a novel regulator of Arf1 activation, controlling Golgi organization and function in anchorage-dependent cells.Summary StatementThis study identifies a role for cell-matrix adhesion in regulating organelle (Golgi) architecture and function which could have implications for multiple cellular pathways and function.

Control of GL2 expression in Arabidopsis leaves and trichomes

Development ◽  
1998 ◽  
Vol 125 (7) ◽  
pp. 1161-1171 ◽  
Author(s):  
D.B. Szymanski ◽  
R.A. Jilk ◽  
S.M. Pollock ◽  
M.D. Marks
Keyword(s):  
Cell Expansion ◽  
Expression Patterns ◽  
Ectopic Expression ◽  
Spatial And Temporal Variation ◽  
R Gene ◽  
Gus Reporter ◽  
Transparent Testa ◽  
Initial Selection ◽  
Epistatic Analysis ◽  
Selection Of

More than twenty genes are required for the correct initiation, spacing, and morphogenesis of trichomes in Arabidopsis. The initial selection of trichome precursors requires the activity of both the GLABROUS1 (GL1) and TRANSPARENT TESTA GLABROUS (TTG) genes. The GLABRA2 (GL2) gene is required for subsequent phases of trichome morphogenesis such as cell expansion, branching, and maturation of the trichome cell wall. Previous studies have shown that GL2 is a member of the homeodomain class of transcription factors. Here we report a detailed analysis of GL2 expression in the shoot using anti-GL2 antibodies and the GUS reporter gene fused to the GL2 promoter. The GL2 expression profile in the shoot is complex, and involves spatial and temporal variation in developing leaves and trichomes. Two separate promoter domains that are expressed in trichomes were identified. GL2, like GL1, is expressed in developing trichomes and in cells surrounding trichomes during early stages of trichome development. Unlike GL1, GL2 expression persists in mature trichomes. It was found that while GL1 and TTG were not required for the initiation of GL2 expression in the non-trichome cells, the presence of a functional GL1 or TTG gene was able to increase GL2 expression in these cells compared to ttg gl1 plants. The hypothesis that GL1 regulates aspects of GL2 expression is consistent with epistatic analysis of gl1 and gl2 and the expression patterns of GL1 and GL2. In support of this hypothesis, it was found that ectopic expression of GL1 in the presence of ectopic expression of the maize R gene, which can bypass the requirement for TTG, can ectopically activate GL2 transcription.

scholarly journals The molecular chaperone Hsp90α deficiency causes retinal degeneration by disrupting Golgi organization and vesicle transportation in photoreceptors

2019 ◽  
Vol 12 (3) ◽  
pp. 216-229 ◽  
Author(s):  
Yuan Wu ◽  
Xiudan Zheng ◽  
Yubo Ding ◽  
Min Zhou ◽  
Zhuang Wei ◽  
...  
Keyword(s):  
Retinal Degeneration ◽  
Molecular Chaperone ◽  
Outer Segment ◽  
Microscopic Analysis ◽  
Heat Shock Protein 90 ◽  
Hsp90 Inhibitor ◽  
Wild Type ◽  
Electron Microscopic ◽  
Golgi Organization ◽  
Deficient Mice

Abstract Heat shock protein 90 (Hsp90) is an abundant molecular chaperone with two isoforms, Hsp90α and Hsp90β. Hsp90β deficiency causes embryonic lethality, whereas Hsp90α deficiency causes few abnormities except male sterility. In this paper, we reported that Hsp90α was exclusively expressed in the retina, testis, and brain. Its deficiency caused retinitis pigmentosa (RP), a disease leading to blindness. In Hsp90α-deficient mice, the retina was deteriorated and the outer segment of photoreceptor was deformed. Immunofluorescence staining and electron microscopic analysis revealed disintegrated Golgi and aberrant intersegmental vesicle transportation in Hsp90α-deficient photoreceptors. Proteomic analysis identified microtubule-associated protein 1B (MAP1B) as an Hsp90α-associated protein in photoreceptors. Hspα deficiency increased degradation of MAP1B by inducing its ubiquitination, causing α-tubulin deacetylation and microtubule destabilization. Furthermore, the treatment of wild-type mice with 17-DMAG, an Hsp90 inhibitor of geldanamycin derivative, induced the same retinal degeneration as Hsp90α deficiency. Taken together, the microtubule destabilization could be the underlying reason for Hsp90α deficiency-induced RP.

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