scholarly journals Diverse Role of SNARE Protein Sec22 in Vesicle Trafficking, Membrane Fusion, and Autophagy

Cells ◽  
2019 ◽  
Vol 8 (4) ◽  
pp. 337 ◽  
Author(s):  
Muhammad Adnan ◽  
Waqar Islam ◽  
Jing Zhang ◽  
Wenhui Zheng ◽  
Guo-Dong Lu
Keyword(s):  
Plasma Membrane ◽  
Membrane Fusion ◽  
Protein Secretion ◽  
Plasma Membranes ◽  
Extracellular Enzymes ◽  
Vesicle Trafficking ◽  
Cellular Systems ◽  
Rnai Pathway ◽  
Snare Protein ◽  
Genetic Redundancy

Protein synthesis begins at free ribosomes or ribosomes attached with the endoplasmic reticulum (ER). Newly synthesized proteins are transported to the plasma membrane for secretion through conventional or unconventional pathways. In conventional protein secretion, proteins are transported from the ER lumen to Golgi lumen and through various other compartments to be secreted at the plasma membrane, while unconventional protein secretion bypasses the Golgi apparatus. Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) proteins are involved in cargo vesicle trafficking and membrane fusion. The ER localized vesicle associated SNARE (v-SNARE) protein Sec22 plays a major role during anterograde and retrograde transport by promoting efficient membrane fusion and assisting in the assembly of higher order complexes by homodimer formation. Sec22 is not only confined to ER–Golgi intermediate compartments (ERGIC) but also facilitates formation of contact sites between ER and plasma membranes. Sec22 mutation is responsible for the development of atherosclerosis and symptoms in the brain in Alzheimer’s disease and aging in humans. In the fruit fly Drosophila melanogaster, Sec22 is essential for photoreceptor morphogenesis, the wingless signaling pathway, and normal ER, Golgi, and endosome morphology. In the plant Arabidopsis thaliana, it is involved in development, and in the nematode Caenorhabditis elegans, it is in involved in the RNA interference (RNAi) pathway. In filamentous fungi, it affects cell wall integrity, growth, reproduction, pathogenicity, regulation of reactive oxygen species (ROS), expression of extracellular enzymes, and transcriptional regulation of many development related genes. This review provides a detailed account of Sec22 function, summarizes its domain structure, discusses its genetic redundancy with Ykt6, discusses what is known about its localization to discrete membranes, its contributions in conventional and unconventional autophagy, and a variety of other roles across different cellular systems ranging from higher to lower eukaryotes, and highlights some of the surprises that have originated from research on Sec22.

scholarly journals Insulin Stimulates Membrane Fusion and GLUT4 Accumulation in Clathrin Coats on Adipocyte Plasma Membranes

2007 ◽  
Vol 27 (9) ◽  
pp. 3456-3469 ◽  
Author(s):  
Shaohui Huang ◽  
Larry M. Lifshitz ◽  
Christine Jones ◽  
Karl D. Bellve ◽  
Clive Standley ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Fusion ◽  
Insulin Signaling ◽  
Plasma Membranes ◽  
Glucose Transporter ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Tirf Microscopy ◽  
Adipocyte Plasma Membranes ◽  
Kinetics Of

ABSTRACT Total internal reflection fluorescence (TIRF) microscopy reveals highly mobile structures containing enhanced green fluorescent protein-tagged glucose transporter 4 (GLUT4) within a zone about 100 nm beneath the plasma membrane of 3T3-L1 adipocytes. We developed a computer program (Fusion Assistant) that enables direct analysis of the docking/fusion kinetics of hundreds of exocytic fusion events. Insulin stimulation increases the fusion frequency of exocytic GLUT4 vesicles by ∼4-fold, increasing GLUT4 content in the plasma membrane. Remarkably, insulin signaling modulates the kinetics of the fusion process, decreasing the vesicle tethering/docking duration prior to membrane fusion. In contrast, the kinetics of GLUT4 molecules spreading out in the plasma membrane from exocytic fusion sites is unchanged by insulin. As GLUT4 accumulates in the plasma membrane, it is also immobilized in punctate structures on the cell surface. A previous report suggested these structures are exocytic fusion sites (Lizunov et al., J. Cell Biol. 169:481-489, 2005). However, two-color TIRF microscopy using fluorescent proteins fused to clathrin light chain or GLUT4 reveals these structures are clathrin-coated patches. Taken together, these data show that insulin signaling accelerates the transition from docking of GLUT4-containing vesicles to their fusion with the plasma membrane and promotes GLUT4 accumulation in clathrin-based endocytic structures on the plasma membrane.

scholarly journals ROLE OF THE GAMETE MEMBRANES IN FERTILIZATION IN SACCOGLOSSUS KOWALEVSKII (ENTEROPNEUSTA)

1963 ◽  
Vol 19 (3) ◽  
pp. 501-518 ◽  
Author(s):  
Laura Hunter Colwin ◽  
Arthur L. Colwin
Keyword(s):  
Plasma Membrane ◽  
Membrane Fusion ◽  
Plasma Membranes ◽  
Sperm Nucleus ◽  
Zygote Formation ◽  
General Hypothesis ◽  
Acrosomal Vesicle ◽  
Saccoglossus Kowalevskii ◽  
Sperm Plasma Membrane

An earlier paper showed that in Saccoglossus the acrosomal tubule makes contact with the egg plasma membrane. The present paper includes evidence that the sperm and egg plasma membranes fuse to establish the single continuous zygote membrane which, consequently, is a mosaic. Contrary to the general hypothesis of Tyler, pinocytosis or phagocytosis plays no role in zygote formation. Contact between the gametes is actually between two newly exposed surfaces: in the spermatozoon, the surface was formerly the interior of the acrosomal vesicle; in the egg, it was membrane previously covered by the egg envelopes. The concept that all the events of fertilization are mediated by a fertilizin-antifertilizin reaction seems an oversimplification of events actually observed: rather, the evidence indicates that a series of specific biochemical interactions probably would be involved. Gamete membrane fusion permits sperm periacrosomal material to meet the egg cytoplasm; if an activating substance exists in the spermatozoon it probably is periacrosomal rather than acrosomal in origin. The contents of the acrosome are expended in the process of delivering the sperm plasma membrane to the egg plasma membrane. After these membranes coalesce, the sperm nucleus and other internal sperm structures move into the egg cytoplasm.

scholarly journals Sphingomyelin Synthase 2, but Not Sphingomyelin Synthase 1, Is Involved in HIV-1 Envelope-mediated Membrane Fusion

2014 ◽  
Vol 289 (44) ◽  
pp. 30842-30856 ◽  
Author(s):  
Yasuhiro Hayashi ◽  
Yoko Nemoto-Sasaki ◽  
Takashi Tanikawa ◽  
Saori Oka ◽  
Kiyoto Tsuchiya ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Fusion ◽  
Actin Polymerization ◽  
Plasma Membranes ◽  
Viral Envelope ◽  
Target Cells ◽  
Nonreceptor Tyrosine Kinase ◽  
Sphingomyelin Synthase ◽  
A Cell ◽  
Hiv 1

Membrane fusion between the viral envelope and plasma membranes of target cells has previously been correlated with HIV-1 infection. Lipids in the plasma membrane, including sphingomyelin, may be crucially involved in HIV-1 infection; however, the role of lipid-metabolic enzymes in membrane fusion remains unclear. In this study, we examined the roles of sphingomyelin synthase (SMS) in HIV-1 Env-mediated membrane fusion using a cell-cell fusion assay with HIV-1 mimetics and their target cells. We employed reconstituted cells as target cells that stably express Sms1 or Sms2 in Sms-deficient cells. Fusion susceptibility was ∼5-fold higher in Sms2-expressing cells (not in Sms1-expressing cells) than in Sms-deficient cells. The enhancement of fusion susceptibility observed in Sms2-expressing cells was reversed and reduced by Sms2 knockdown. We also found that catalytically nonactive Sms2 promoted membrane fusion susceptibility. Moreover, SMS2 co-localized and was constitutively associated with the HIV receptor·co-receptor complex in the plasma membrane. In addition, HIV-1 Env treatment resulted in a transient increase in nonreceptor tyrosine kinase (Pyk2) phosphorylation in Sms2-expressing and catalytically nonactive Sms2-expressing cells. We observed that F-actin polymerization in the region of membrane fusion was more prominent in Sms2-expressing cells than Sms-deficient cells. Taken together, our research provides insight into a novel function of SMS2 which is the regulation of HIV-1 Env-mediated membrane fusion via actin rearrangement.

scholarly journals Cytoskeletal reorganization and plasma membrane fusion in conjugating Tetrahymena

1985 ◽  
Vol 73 (1) ◽  
pp. 69-85
Author(s):  
J. Wolfe
Keyword(s):  
Plasma Membrane ◽  
Membrane Fusion ◽  
Plasma Membranes ◽  
Matrix Material ◽  
Thick Layer ◽  
Skeletal Structure ◽  
Mating Types ◽  
Skeletal Element ◽  
Thin Sections ◽  
Ionic Detergent

The conjugation junction of Tetrahymena is the specialized site where plasma membrane fusion occurs between two cells of complementary mating types. The junction is constructed through a series of cooperative interactions and morphogenetic steps. A contact-mediated interaction between free-swimming, sexually mature and mating-competent cells of two complementary mating types induces a morphological transformation of the anterior tips. Cells then join in pairs aligned by the apposition of their modified tips. Thin sections show that the plasma membranes of the tips are separated by approximately 500 A of extracellular space, in which some strands of matrix material can be identified. The cytoplasmic face of the membrane is in contact with a junction-specific thick layer of electron-dense material. At hundreds of independent sites in this junction plasma membranes fuse in a limited manner, thereby establishing hundreds of separate membrane-ensheathed cytoplasmic channels that connect the two cells. At the same locations the thick submembrane layer is interrupted. Consequently, the junction appears to be a structure that is perforated with hundreds of pores. This study poses the question of whether the junction's submembrane layer is, or includes, a skeletal element. Cells were extracted with the non-ionic detergent Triton X-100 under conditions that yield cytoskeletal frameworks (CFs) that maintain the morphological integrity of the cells. The CFs include chromatin and also cortical structures such as microtubule bands, basal bodies, ciliary axonemes, kinetodesmal fibres and fibrillar epiplasm. CFs of conjugant pairs are also paired, indicating that the junction contains a skeletal element that is responsible for integrating the individual CFs into a higher-order complex. At the ultrastructural level the skeletal structure of the junction includes membrane lamina and a submembrane scaffold, residues of the plasma membrane and thick submembrane layer, respectively, both of which are interrupted at the pores. However, the two separate scaffolds are joined at the rims of the pores. This provides a means by which the separate CFs become integrated. On the basis of images of junctional CFs, which show interruptions of the scaffold without concomitant membrane fusion, but where laminae are pressed close together, a specific model of membrane fusion is proposed. According to this model, the submembrane skeletal scaffold regulates membrane fusion by limiting its occurrence, and the extent of its occurrence.

scholarly journals Prm1 Targeting to Contact Sites Enhances Fusion during Mating in Saccharomyces cerevisiae

2010 ◽  
Vol 9 (10) ◽  
pp. 1538-1548 ◽  
Author(s):  
Valerie N. Olmo ◽  
Eric Grote
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Membrane Fusion ◽  
Intracellular Transport ◽  
Plasma Membranes ◽  
Yeast Cells ◽  
Fusion Event ◽  
Mating Activity ◽  
Content Type ◽  
Contact Sites

ABSTRACT Prm1 is a pheromone-regulated membrane glycoprotein involved in the plasma membrane fusion event of Saccharomyces cerevisiae mating. Although this function suggests that Prm1 should act at contact sites in pairs of mating yeast cells where plasma membrane fusion occurs, only a small percentage of the total Prm1 was actually detected on the plasma membrane. We therefore investigated the intracellular transport of Prm1 and how this transport contributes to cell fusion. Two Prm1 chimeras that were sorted away from the contact site had reduced fusion activity, indicating that Prm1 indeed functions at contact sites. However, most Prm1 is located in endosomes and other cytoplasmic organelles and is targeted to vacuoles for degradation. Mutations in a putative endocytosis signal in a cytoplasmic loop partially stabilized the Prm1 protein and caused it to accumulate on the plasma membrane, but this endocytosis mutant actually had reduced mating activity. When Prm1 was expressed from a galactose-regulated promoter and its synthesis was repressed at the start of mating, vanishingly small amounts of Prm1 protein remained at the time when the plasma membranes came into contact. Nevertheless, this stable pool of Prm1 was retained at polarized sites on the plasma membrane and was sufficient to promote plasma membrane fusion. Thus, the amount of Prm1 expressed in mating yeast is far in excess of the amount required to facilitate fusion.

scholarly journals SNAREs: Could They be the Answer to an Energy Landscape Riddle in Exocytosis?

2010 ◽  
Vol 10 ◽  
pp. 1258-1268 ◽  
Author(s):  
Wei Liu ◽  
Vladimir Parpura
Keyword(s):  
Plasma Membrane ◽  
Membrane Fusion ◽  
Plasma Membranes ◽  
Surface Force ◽  
Snare Complex ◽  
Titration Calorimetry ◽  
Force Microscopy ◽  
Atomic Force ◽  
Experimental Approaches ◽  
Intracellular Organelles

During exocytosis, chemical transmitters stored in secretory vesicles can be released upon fusion of these intracellular organelles to the plasma membrane. In this process, SNARE proteins that form a ternary core complex play a central role. This complex could provide the means for generation/storage of energy necessary for driving the fusion of vesicular and plasma membranes. Recently, the amount of energy for (dis)assembly of the ternary complex has been measured using various experimental approaches, including atomic force microscopy, the surface force apparatus, and isothermal titration calorimetry. The obtained measurements are in good agreement with the calculated energy required for membrane fusion achieved by theoretical modeling approaches. Whether the energy expenditure to form the ternary SNARE complex can be utilized towards membrane fusion and/or docking/tethering of vesicles to the plasma membrane still remains one of the key contemporary issues in biophysics and neuroscience.

scholarly journals Prm1p, a Pheromone-Regulated Multispanning Membrane Protein, Facilitates Plasma Membrane Fusion during Yeast Mating

2000 ◽  
Vol 151 (3) ◽  
pp. 719-730 ◽  
Author(s):  
Maxwell G. Heiman ◽  
Peter Walter
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Membrane Fusion ◽  
Cell Fusion ◽  
Plasma Membranes ◽  
Molecular Mechanisms ◽  
Transmembrane Protein ◽  
Large Fraction ◽  
Cell Contact ◽  
Yeast Mating

Cell fusion occurs throughout development, from fertilization to organogenesis. The molecular mechanisms driving plasma membrane fusion in these processes remain unknown. While yeast mating offers an excellent model system in which to study cell fusion, all genes previously shown to regulate the process act at or before cell wall breakdown; i.e., well before the two plasma membranes have come in contact. Using a new strategy in which genomic data is used to predict which genes may possess a given function, we identified PRM1, a gene that is selectively expressed during mating and that encodes a multispanning transmembrane protein. Prm1p localizes to sites of cell–cell contact where fusion occurs. In matings between Δprm1 mutants, a large fraction of cells initiate zygote formation and degrade the cell wall separating mating partners but then fail to fuse. Electron microscopic analysis reveals that the two plasma membranes in these mating pairs are tightly apposed, remaining separated only by a uniform gap of ∼8 nm. Thus, the phenotype of Δprm1 mutants defines a new step in the mating reaction in which membranes are juxtaposed, possibly through a defined adherence junction, yet remain unfused. This phenotype suggests a role for Prm1p in plasma membrane fusion.

scholarly journals A specific interaction in vitro between pancreatic zymogen granules and plasma membranes: stimulation by G-protein activators but not by Ca2+.

1989 ◽  
Vol 109 (6) ◽  
pp. 2801-2808 ◽  
Author(s):  
C Y Nadin ◽  
J Rogers ◽  
S Tomlinson ◽  
J M Edwardson
Keyword(s):  
Plasma Membrane ◽  
Membrane Fusion ◽  
G Protein ◽  
G Proteins ◽  
Plasma Membranes ◽  
Specific Interaction ◽  
Zymogen Granules ◽  
Fusion Event ◽  
A Cell

The molecular details of the final step in the process of regulated exocytosis, the fusion of the membrane of the secretory granule with the plasma membrane, are at present obscure. As a first step in an investigation of this membrane fusion event, we have developed a cell-free assay for the interaction between pancreatic zymogen granules and plasma membranes. We show here that plasma membranes are able to trigger the release of the granule contents, and that this effect is specific to pancreatic membranes, involves membrane fusion, requires membrane proteins, and is stimulated by activators of G-proteins but not by Ca2+. The assay is simple, reliable, and rapid, and should permit the identification of proteins that are involved in the exocytotic fusion event.

Membrane microdomains: lessons from microscopy

1995 ◽  
Vol 53 ◽  
pp. 776-777
Author(s):  
J.M. Robinson ◽  
J.M Oliver
Keyword(s):  
Spatial Distribution ◽  
Plasma Membrane ◽  
Epithelial Cells ◽  
Plasma Membranes ◽  
Cell Types ◽  
Imaging Modalities ◽  
Membrane Microdomains ◽  
Membrane Domains ◽  
Lateral Heterogeneity ◽  
Functional Importance

Specialized regions of plasma membranes displaying lateral heterogeneity are the focus of this Symposium. Specialized membrane domains are known for certain cell types such as differentiated epithelial cells where lateral heterogeneity in lipids and proteins exists between the apical and basolateral portions of the plasma membrane. Lateral heterogeneity and the presence of microdomains in membranes that are uniform in appearance have been more difficult to establish. Nonetheless a number of studies have provided evidence for membrane microdomains and indicated a functional importance for these structures.This symposium will focus on the use of various imaging modalities and related approaches to define membrane microdomains in a number of cell types. The importance of existing as well as emerging imaging technologies for use in the elucidation of membrane microdomains will be highlighted. The organization of membrane microdomains in terms of dimensions and spatial distribution is of considerable interest and will be addressed in this Symposium.

Pore-Spanning Plasma Membranes Derived from Giant Plasma Membrane Vesicles

2021 ◽  
Author(s):  
Nikolas K. Teiwes ◽  
Ingo Mey ◽  
Phila C. Baumann ◽  
Lena Strieker ◽  
Ulla Unkelbach ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Plasma Membranes ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles
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