scholarly journals The chlamydial deubiquitinase Cdu1 supports recruitment of Golgi vesicles to the inclusion

2020 ◽  
Vol 22 (5) ◽  
Author(s):  
Daniela Auer ◽  
Sophie D. Hügelschäffer ◽  
Annette B. Fischer ◽  
Thomas Rudel
Keyword(s):  
Golgi Vesicles

Golgi Apparatus and Melanogenesis: Ultrastructural Study of a Human Cellular Blue Nevus (Melanocytoma)

1973 ◽  
Vol 31 ◽  
pp. 380-381
Author(s):  
S.R. Allegra
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Ultrastructural Study ◽  
The Other ◽  
Blue Nevus ◽  
Normal Complement ◽  
Golgi Vesicles ◽  
Golgi System ◽  
The Subject ◽  
Cellular Blue Nevus

The respective roles of the ribo somes, endoplasmic reticulum, Golgi apparatus and perhaps nucleus in the synthesis and maturation of melanosomes is still the subject of some controversy. While the early melanosomes (premelanosomes) have been frequently demonstrated to originate as Golgi vesicles, it is undeniable that these structures can be formed in cells in which Golgi system is not found. This report was prompted by the findings in an essentially amelanotic human cellular blue nevus (melanocytoma) of two distinct lines of melanocytes one of which was devoid of any trace of Golgi apparatus while the other had normal complement of this organelle.

MEMBRANE-PROTEIN AUTOPHOSPHORYLATION IN RAT MAMMARY GOLGI VESICLES

1981 ◽  
Vol 9 (2) ◽  
pp. 137P-137P
Author(s):  
David W. West ◽  
Roger A. Clegg
Keyword(s):  
Membrane Protein ◽  
Golgi Vesicles

scholarly journals Divalent cation activation of galactosyltransferase in native mammary Golgi vesicles.

1990 ◽  
Vol 265 (26) ◽  
pp. 15731-15737 ◽  
Author(s):  
D.L. Witsell ◽  
C.E. Casey ◽  
M.C. Neville
Keyword(s):  
Divalent Cation ◽  
Golgi Vesicles ◽  
Cation Activation

Golvesin-GFP fusions as distinct markers for Golgi and post-Golgi vesicles in Dictyostelium cells

2000 ◽  
Vol 92 (7) ◽  
pp. 495-511 ◽  
Author(s):  
Natalie Schneider ◽  
Jean-Marc Schwartz ◽  
Jana Köhler ◽  
Michael Becker ◽  
Heinz Schwarz ◽  
...  
Keyword(s):  
Golgi Vesicles

scholarly journals Vaccinia Virus F13L Protein with a Conserved Phospholipase Catalytic Motif Induces Colocalization of the B5R Envelope Glycoprotein in Post-Golgi Vesicles

2001 ◽  
Vol 75 (16) ◽  
pp. 7528-7542 ◽  
Author(s):  
Matloob Husain ◽  
Bernard Moss
Keyword(s):  
Vaccinia Virus ◽  
Fluorescent Protein ◽  
Plasmid Vector ◽  
Recombinant Vaccinia Virus ◽  
Open Reading Frames ◽  
Type I ◽  
Golgi Vesicles ◽  
Infected Cells ◽  
Catalytic Motif ◽  
Green Fluorescent

ABSTRACT The wrapping of intracellular mature vaccinia virions by modifiedtrans-Golgi or endosomal cisternae to form intracellular enveloped virions is dependent on at least two viral proteins encoded by the B5R and F13L open reading frames. B5R is a type I integral membrane glycoprotein, whereas F13L is an unglycosylated, palmitylated protein with a motif that is conserved in a superfamily of phospholipid-metabolizing enzymes. Microscopic visualization of the F13L protein was achieved by fusing it to the enhanced green fluorescent protein (GFP). F13L-GFP was functional when expressed by a recombinant vaccinia virus in which it replaced the wild-type F13L gene or by transfection of uninfected cells with a plasmid vector followed by infection with an F13L deletion mutant. In uninfected or infected cells, F13L-GFP was associated with Golgi cisternae and post-Golgi vesicles containing the LAMP 2 late endosomal-lysosomal marker. Association of F13L-GFP with vesicles was dependent on an intact phospholipase catalytic motif and sites of palmitylation. The B5R protein was also associated with LAMP2-containing vesicles when F13L-GFP was coexpressed, but was largely restricted to Golgi cisternae in the absence of F13L-GFP or when the F13L moiety was mutated. We suggest that the F13L protein, like its human phospholipase D homolog, regulates vesicle formation and that this process is involved in intracellular enveloped virion membrane formation.

scholarly journals Role of the Gag Matrix Domain in Targeting Human Immunodeficiency Virus Type 1 Assembly

2000 ◽  
Vol 74 (6) ◽  
pp. 2855-2866 ◽  
Author(s):  
Akira Ono ◽  
Jan M. Orenstein ◽  
Eric O. Freed
Keyword(s):  
Human Immunodeficiency Virus ◽  
Plasma Membrane ◽  
Virus Particle ◽  
Particle Formation ◽  
Membrane Targeting ◽  
Basic Domain ◽  
Golgi Vesicles ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACT Human immunodeficiency virus type 1 (HIV-1) particle formation and the subsequent initiation of protease-mediated maturation occur predominantly on the plasma membrane. However, the mechanism by which HIV-1 assembly is targeted specifically to the plasma membrane versus intracellular membranes is largely unknown. Previously, we observed that mutations between residues 84 and 88 of the matrix (MA) domain of HIV-1 Gag cause a retargeting of virus particle formation to an intracellular site. In this study, we demonstrate that the mutant virus assembly occurs in the Golgi or in post-Golgi vesicles. These particles undergo core condensation in a protease-dependent manner, indicating that virus maturation can occur not only on the plasma membrane but also in the Golgi or post-Golgi vesicles. The intracellular assembly of mutant particles is dependent on Gag myristylation but is not influenced by p6Gag or envelope glycoprotein expression. Previous characterization of viral revertants suggested a functional relationship between the highly basic domain of MA (amino acids 17 to 31) and residues 84 to 88. We now demonstrate that mutations in the highly basic domain also retarget virus particle formation to the Golgi or post-Golgi vesicles. Although the basic domain has been implicated in Gag membrane binding, no correlation was observed between the impact of mutations on membrane binding and Gag targeting, indicating that these two functions of MA are genetically separable. Plasma membrane targeting of Gag proteins with mutations in either the basic domain or between residues 84 and 88 was rescued by coexpression with wild-type Gag; however, the two groups of MA mutants could not rescue each other. We propose that the highly basic domain of MA contains a major determinant of HIV-1 Gag plasma membrane targeting and that mutations between residues 84 and 88 disrupt plasma membrane targeting through an effect on the basic domain.

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