The Use of Liposomes to Study COPII- and COPI-Coated Vesicle Formation and Membrane Protein Sorting

Methods ◽  
2000 ◽  
Vol 20 (4) ◽  
pp. 417-428 ◽  
Author(s):  
Ken Matsuoka ◽  
Randy Schekman
Keyword(s):  
Membrane Protein ◽  
Protein Sorting ◽  
Coated Vesicle ◽  
Vesicle Formation

scholarly journals Human ESCRT-II Complex and Its Role in Human Immunodeficiency Virus Type 1 Release

2006 ◽  
Vol 80 (19) ◽  
pp. 9465-9480 ◽  
Author(s):  
Charles Langelier ◽  
Uta K. von Schwedler ◽  
Robert D. Fisher ◽  
Ivana De Domenico ◽  
Paul L. White ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Protein Sorting ◽  
Growth Factor Receptor ◽  
Multivesicular Body ◽  
Vesicle Formation ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACT The budding of many enveloped RNA viruses, including human immunodeficiency virus type 1 (HIV-1), requires some of the same cellular machinery as vesicle formation at the multivesicular body (MVB). In Saccharomyces cerevisiae, the ESCRT-II complex performs a central role in MVB protein sorting and vesicle formation, as it is recruited by the upstream ESCRT-I complex and nucleates assembly of the downstream ESCRT-III complex. Here, we report that the three subunits of human ESCRT-II, EAP20, EAP30, and EAP45, have a number of properties in common with their yeast orthologs. Specifically, EAP45 bound ubiquitin via its N-terminal GRAM-like ubiquitin-binding in EAP45 (GLUE) domain, both EAP45 and EAP30 bound the C-terminal domain of TSG101/ESCRT-I, and EAP20 bound the N-terminal half of CHMP6/ESCRT-III. Consistent with its expected role in MVB vesicle formation, (i) human ESCRT-II localized to endosomal membranes in a VPS4-dependent fashion and (ii) depletion of EAP20/ESCRT-II and CHMP6/ESCRT-III inhibited lysosomal targeting and downregulation of the epidermal growth factor receptor, albeit to a lesser extent than depletion of TSG101/ESCRT-I. Nevertheless, HIV-1 release and infectivity were not reduced by efficient small interfering RNA depletion of EAP20/ESCRT-II or CHMP6/ESCRT-III. These observations indicate that there are probably multiple pathways for protein sorting/MVB vesicle formation in human cells and that HIV-1 does not utilize an ESCRT-II-dependent pathway to leave the cell.

scholarly journals Cytosolic ARFs are required for vesicle formation but not for cell-free intra-Golgi transport: evidence for coated vesicle-independent transport.

1994 ◽  
Vol 5 (2) ◽  
pp. 237-252 ◽  
Author(s):  
T C Taylor ◽  
M Kanstein ◽  
P Weidman ◽  
P Melançon
Keyword(s):  
Chinese Hamster Ovary ◽  
Chinese Hamster ◽  
Specific Inhibitor ◽  
Coated Vesicles ◽  
Coated Vesicle ◽  
Vesicle Formation ◽  
Golgi Transport ◽  
Independent Mechanism ◽  
Free Transport

We investigated the role of ADP-ribosylation factors (ARFs) in Golgi function using biochemical and morphological cell-free assays. An ARF-free cytosol produced from soluble Chinese hamster ovary (CHO) extracts supports intra-Golgi transport by a mechanism that is biochemically indistinguishable from control transport reactions: ARF-free transport reactions are NSF-dependent, remain sensitive to the donor Golgi-specific inhibitor ilimaquinone, and exhibit kinetics that are identical to that of control reactions containing ARFs. In contrast, ARF-free cytosol does not support the formation of coated vesicles on Golgi cisternae. However, vesicle formation is reconstituted upon the addition of ARF1. These data suggest that neither soluble ARFs nor coated vesicle formation are essential for transport. We conclude that cell-free intra-Golgi transport proceeds via a coated vesicle-independent mechanism regardless of vesicle formation on Golgi cisternae.

scholarly journals COPII-Coated Vesicle Formation Reconstituted with Purified Coat Proteins and Chemically Defined Liposomes

Cell ◽  
1998 ◽  
Vol 93 (2) ◽  
pp. 263-275 ◽  
Author(s):  
Ken Matsuoka ◽  
Lelio Orci ◽  
Mylène Amherdt ◽  
Sebastian Y Bednarek ◽  
Susan Hamamoto ◽  
...  
Keyword(s):  
Coated Vesicle ◽  
Vesicle Formation ◽  
Coat Proteins

Clathrin: the molecular shape shifter

2021 ◽  
Vol 478 (16) ◽  
pp. 3099-3123
Author(s):  
Katherine M. Wood ◽  
Corinne J. Smith
Keyword(s):  
Cell Migration ◽  
Molecular Shape ◽  
Coated Vesicle ◽  
Vesicle Formation ◽  
Lattice Structures ◽  
Tubular Structures ◽  
Cellular Functions ◽  
Diverse Range ◽  
Cellular Processes ◽  
Vesicle Recycling

Clathrin is best known for its contribution to clathrin-mediated endocytosis yet it also participates to a diverse range of cellular functions. Key to this is clathrin's ability to assemble into polyhedral lattices that include curved football or basket shapes, flat lattices or even tubular structures. In this review, we discuss clathrin structure and coated vesicle formation, how clathrin is utilised within different cellular processes including synaptic vesicle recycling, hormone desensitisation, spermiogenesis, cell migration and mitosis, and how clathrin's remarkable ‘shapeshifting’ ability to form diverse lattice structures might contribute to its multiple cellular functions.

scholarly journals Temporal Ordering in Endocytic Clathrin-Coated Vesicle Formation via AP2 Phosphorylation

2019 ◽  
Vol 50 (4) ◽  
pp. 494-508.e11 ◽  
Author(s):  
Antoni G. Wrobel ◽  
Zuzana Kadlecova ◽  
Jan Kamenicky ◽  
Ji-Chun Yang ◽  
Torsten Herrmann ◽  
...  
Keyword(s):  
Coated Vesicle ◽  
Vesicle Formation ◽  
Temporal Ordering

Protein Sorting in Healthy and Diseased Photoreceptors

2019 ◽  
Vol 5 (1) ◽  
pp. 73-98 ◽  
Author(s):  
Yoshikazu Imanishi
Keyword(s):  
Signal Transduction ◽  
Membrane Protein ◽  
Outer Segment ◽  
Protein Sorting ◽  
Rods And Cones ◽  
Retinal Photoreceptor ◽  
Photoreceptor Neurons ◽  
Cellular Compartments ◽  
G Protein Coupled ◽  
Distinct Membrane

Rods and cones are retinal photoreceptor neurons required for our visual sensation. Because of their highly polarized structures and well-characterized processes of G protein–coupled receptor–mediated phototransduction signaling, these photoreceptors have been excellent models for studying the compartmentalization and sorting of proteins. Rods and cones have a modified ciliary compartment called the outer segment (OS) as well as non-OS compartments. The distinct membrane protein compositions between OS and non-OS compartments suggest that the OS is separated from the rest of the cellular compartments by multiple barriers or gates that are selectively permissive to specific cargoes. This review discusses the mechanisms of protein sorting and compartmentalization in photoreceptor neurons. Proper sorting and compartmentalization of membrane proteins are required for signal transduction and transmission. This review also discusses the roles of compartmentalized signaling, which is compromised in various retinal ciliopathies.

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