scholarly journals Cargo induces retromer-mediated membrane remodeling on membranes

2018 ◽  
Vol 29 (22) ◽  
pp. 2709-2719 ◽  
Author(s):  
Latha Kallur Purushothaman ◽  
Christian Ungermann
Keyword(s):  
Plasma Membrane ◽  
Simple Model ◽  
Membrane Proteins ◽  
Golgi Complex ◽  
Exact Order ◽  
Membrane Remodeling ◽  
Sorting Nexin ◽  
Low Concentrations ◽  
Sorting Station ◽  
Specific Trigger

Endosomes serve as a central sorting station of lipids and proteins that arrive via vesicular carrier from the plasma membrane and the Golgi complex. At the endosome, retromer complexes sort selected receptors and membrane proteins into tubules or vesicles that bud off the endosome. The mature endosome finally fuses with the lysosome. Retromer complexes consist of a cargo selection complex (CSC) and a membrane remodeling part (sorting nexin [SNX]-Bin/amphiphysin/Rvs [BAR], or Snx3 in yeast) and different assemblies of retromer mediate recycling of different cargoes. Due to this complexity, the exact order of events that results in carrier formation is not yet understood. Here, we reconstituted this process on giant unilamellar vesicles together with purified retromer complexes from yeast and selected cargoes. Our data reveal that the membrane remodeling activity of both Snx3 and the SNX-BAR complex is strongly reduced at low concentrations, which can be reactivated by CSC. At even lower concentrations, these complexes still associate with membranes, but only remodel membranes in the presence of their specific cargoes. Our data thus favor a simple model, where cargo functions as a specific trigger of retromer-mediated sorting on endosomes.

scholarly journals Segregation in the Golgi complex precedes export of endolysosomal proteins in distinct transport carriers

2017 ◽  
Vol 216 (12) ◽  
pp. 4141-4151 ◽  
Author(s):  
Yu Chen ◽  
David C. Gershlick ◽  
Sang Yoon Park ◽  
Juan S. Bonifacino
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Golgi Complex ◽  
Adaptor Proteins ◽  
Transmembrane Domains ◽  
The Other ◽  
Present Evidence ◽  
Sorting Signals ◽  
Vesicular Carriers ◽  
Classical Models

Biosynthetic sorting of newly synthesized transmembrane cargos to endosomes and lysosomes is thought to occur at the TGN through recognition of sorting signals in the cytosolic tails of the cargos by adaptor proteins, leading to cargo packaging into coated vesicles destined for the endolysosomal system. Here we present evidence for a different mechanism in which two sets of endolysosomal proteins undergo early segregation to distinct domains of the Golgi complex by virtue of the proteins’ luminal and transmembrane domains. Proteins in one Golgi domain exit into predominantly vesicular carriers by interaction of sorting signals with adaptor proteins, but proteins in the other domain exit into predominantly tubular carriers shared with plasma membrane proteins, independently of signal–adaptor interactions. These findings demonstrate that sorting of endolysosomal proteins begins at an earlier stage and involves mechanisms that partly differ from those described by classical models.

The trans-most cisternae of the Golgi complex: A compartment for sorting of secretory and plasma membrane proteins

Cell ◽  
1987 ◽  
Vol 51 (6) ◽  
pp. 1039-1051 ◽  
Author(s):  
Lelio Orci ◽  
Mariella Ravazzola ◽  
Mylene Amherdt ◽  
Alain Perrelet ◽  
Sharon K. Powell ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Golgi Complex ◽  
Plasma Membrane Proteins

scholarly journals COPI mediates recycling of an exocytic SNARE from endosomes by recognition of a ubiquitin sorting signal

2017 ◽  
Author(s):  
Peng Xu ◽  
Hannah M. Hankins ◽  
Chris Macdonald ◽  
Samuel J. Erlinger ◽  
Meredith N. Frazier ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Golgi Complex ◽  
Budding Yeast ◽  
Sorting Signal ◽  
Binding Domains ◽  
Transport Vesicles ◽  
Early Endosomes ◽  
Ubiquitin Binding ◽  
Target Membrane

ABSTRACTThe COPI coat forms transport vesicles from the Golgi complex and plays a poorly defined role in endocytic trafficking. Here we show that COPI mediates delivery of a budding yeast SNARE (Snc1) from early endosomes to the Golgi complex through recognition of a polyubiquitin sorting signal. Snc1 is a v-SNARE that drives fusion of exocytic vesicles with the plasma membrane, and then recycles through early endosomes back to the Golgi for reuse. Removal of ubiquitin from Snc1, or deletion of a β’-COP subunit propeller domain that binds K63-linked polyubiquitin, causes aberrant accumulation of Snc1 in early endosomes. Moreover, replacement of the β’-COP propeller domain with unrelated ubiquitin-binding domains restores Snc1 recycling. These results indicate that ubiquitination, a modification well known to target membrane proteins to the lysosome or vacuole for degradation, can also function as recycling signal to sort a SNARE into COPI vesicles at early endosomes for Golgi delivery.

scholarly journals COPI mediates recycling of an exocytic SNARE by recognition of a ubiquitin sorting signal

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Peng Xu ◽  
Hannah M Hankins ◽  
Chris MacDonald ◽  
Samuel J Erlinger ◽  
Meredith N Frazier ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Golgi Complex ◽  
Endocytic Pathway ◽  
Endocytic Trafficking ◽  
Degradative Pathway ◽  
Binding Domains ◽  
Transport Vesicles ◽  
Ubiquitin Binding ◽  
Target Membrane

The COPI coat forms transport vesicles from the Golgi complex and plays a poorly defined role in endocytic trafficking. Here we show that COPI binds K63-linked polyubiquitin and this interaction is crucial for trafficking of a ubiquitinated yeast SNARE (Snc1). Snc1 is a v-SNARE that drives fusion of exocytic vesicles with the plasma membrane, and then recycles through the endocytic pathway to the Golgi for reuse in exocytosis. Removal of ubiquitin from Snc1, or deletion of a β'-COP subunit propeller domain that binds K63-linked polyubiquitin, disrupts Snc1 recycling causing aberrant accumulation in internal compartments. Moreover, replacement of the β'-COP propeller domain with unrelated ubiquitin-binding domains restores Snc1 recycling. These results indicate that ubiquitination, a modification well known to target membrane proteins to the lysosome or vacuole for degradation, can also function as recycling signal to sort a SNARE into COPI vesicles in a non-degradative pathway.

Changes Occur in Plasma Membrane Turnover when K562 Leukemia Cells are Induced to Differentiate

1982 ◽  
Vol 40 ◽  
pp. 286-287
Author(s):  
L. M. Marshall
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Intracellular Transport ◽  
Parent Cell ◽  
Membrane Turnover ◽  
Coated Pits ◽  
Surface Distribution ◽  
Specific Proteins ◽  
Erythroleukemic Cell ◽  
Specific Membrane

A human erythroleukemic cell line, metabolically blocked in a late stage of erythropoiesis, becomes capable of differentiation along the normal pathway when grown in the presence of hemin. This process is characterized by hemoglobin synthesis followed by rearrangement of the plasma membrane proteins and culminates in asymmetrical cytokinesis in the absence of nuclear division. A reticulocyte-like cell buds from the nucleus-containing parent cell after erythrocyte specific membrane proteins have been sequestered into its membrane. In this process the parent cell faces two obstacles. First, to organize its erythrocyte specific proteins at one pole of the cell for inclusion in the reticulocyte; second, to reduce or abolish membrane protein turnover since hemoglobin is virtually the only protein being synthesized at this stage. A means of achieving redistribution and cessation of turnover could involve movement of membrane proteins by a directional lipid flow. Generation of a lipid flow towards one pole and accumulation of erythrocyte-specific membrane proteins could be achieved by clathrin coated pits which are implicated in membrane endocytosis, intracellular transport and turnover. In non-differentiating cells, membrane proteins are turned over and are random in surface distribution. If, however, the erythrocyte specific proteins in differentiating cells were excluded from endocytosing coated pits, not only would their turnover cease, but they would also tend to drift towards and collect at the site of endocytosis. This hypothesis requires that different protein species are endocytosed by the coated vesicles in non-differentiating than by differentiating cells.

Detergent fractionation with subsequent subtractive suppression hybridization as a tool for identifying genes coding for plasma membrane proteins

2009 ◽  
Vol 18 (6) ◽  
pp. 527-535 ◽  
Author(s):  
Andreas Lange ◽  
Claudia Kistler ◽  
Tanja B. Jutzi ◽  
Alexandr V. Bazhin ◽  
Claus Detlev Klemke ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Proteins ◽  
Plasma Membrane Proteins ◽  
Subtractive Suppression Hybridization

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 Correlative AFM and fluorescence imaging demonstrate nanoscale membrane remodeling and ring-like and tubular structure formation by septins

Nanoscale ◽  
2021 ◽  
Author(s):  
Anthony Vial ◽  
Cyntia Taveneau ◽  
Luca Costa ◽  
brieuc chauvin ◽  
hussein nasrallah ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Division ◽  
Structure Formation ◽  
Fluorescence Imaging ◽  
Tubular Structure ◽  
Membrane Remodeling

Septins are ubiquitous cytoskeletal filaments that interact with the inner plasma membrane and are essential for cell division in eukaryotes. In cellular contexts, septins are often localized at micrometric gaussian...

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