scholarly journals Dynein-mediated transport and membrane trafficking control PAR3 polarised distribution

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Julie Jouette ◽  
Antoine Guichet ◽  
Sandra B Claret
Keyword(s):  
Plasma Membrane ◽  
Cell Polarity ◽  
Membrane Trafficking ◽  
Control Cell ◽  
Vesicular Trafficking ◽  
Second Phase ◽  
Membrane Domains ◽  
Anterior Cortex ◽  
Essential Proteins ◽  
Dynein Motor

The scaffold protein PAR3 and the kinase PAR1 are essential proteins that control cell polarity. Their precise opposite localisations define plasma membrane domains with specific functions. PAR3 and PAR1 are mutually inhibited by direct or indirect phosphorylations, but their fates once phosphorylated are poorly known. Through precise spatiotemporal quantification of PAR3 localisation in the Drosophila oocyte, we identify several mechanisms responsible for its anterior cortex accumulation and its posterior exclusion. We show that PAR3 posterior plasma membrane exclusion depends on PAR1 and an endocytic mechanism relying on RAB5 and PI(4,5)P2. In a second phase, microtubules and the dynein motor, in connection with vesicular trafficking involving RAB11 and IKK-related kinase, IKKε, are required for PAR3 transport towards the anterior cortex. Altogether, our results point to a connection between membrane trafficking and dynein-mediated transport to sustain PAR3 asymmetry.

scholarly journals CAPS and Munc13 utilize distinct PIP2-linked mechanisms to promote vesicle exocytosis

2014 ◽  
Vol 25 (4) ◽  
pp. 508-521 ◽  
Author(s):  
Greg Kabachinski ◽  
Masaki Yamaga ◽  
D. Michelle Kielar-Grevstad ◽  
Stephen Bruinsma ◽  
Thomas F. J. Martin
Keyword(s):  
Spatial Distribution ◽  
Plasma Membrane ◽  
Membrane Trafficking ◽  
Total Internal Reflection ◽  
Vesicle Fusion ◽  
Live Cells ◽  
Membrane Domains ◽  
Direct View ◽  
Vesicle Exocytosis ◽  
Dependent Protein

Phosphoinositides provide compartment-specific signals for membrane trafficking. Plasma membrane phosphatidylinositol 4,5-bisphosphate (PIP2) is required for Ca2+-triggered vesicle exocytosis, but whether vesicles fuse into PIP2-rich membrane domains in live cells and whether PIP2 is metabolized during Ca2+-triggered fusion were unknown. Ca2+-dependent activator protein in secretion 1 (CAPS-1; CADPS/UNC31) and ubMunc13-2 (UNC13B) are PIP2-binding proteins required for Ca2+-triggered vesicle exocytosis in neuroendocrine PC12 cells. These proteins are likely effectors for PIP2, but their localization during exocytosis had not been determined. Using total internal reflection fluorescence microscopy in live cells, we identify PIP2-rich membrane domains at sites of vesicle fusion. CAPS is found to reside on vesicles but depends on plasma membrane PIP2 for its activity. Munc13 is cytoplasmic, but Ca2+-dependent translocation to PIP2-rich plasma membrane domains is required for its activity. The results reveal that vesicle fusion into PIP2-rich membrane domains is facilitated by sequential PIP2-dependent activation of CAPS and PIP2-dependent recruitment of Munc13. PIP2 hydrolysis only occurs under strong Ca2+ influx conditions sufficient to activate phospholipase Cη2 (PLCη2). Such conditions reduce CAPS activity and enhance Munc13 activity, establishing PLCη2 as a Ca2+-dependent modulator of exocytosis. These studies provide a direct view of the spatial distribution of PIP2 linked to vesicle exocytosis via regulation of lipid-dependent protein effectors CAPS and Munc13.

Steps in the morphogenesis of a polarized epithelium. II. Disassembly and assembly of plasma membrane domains during reversal of epithelial cell polarity in multicellular epithelial (MDCK) cysts

1990 ◽  
Vol 95 (1) ◽  
pp. 153-165
Author(s):  
A.Z. Wang ◽  
G.K. Ojakian ◽  
W.J. Nelson
Keyword(s):  
Plasma Membrane ◽  
Suspension Culture ◽  
Cell Polarity ◽  
Collagen Gel ◽  
Preceding Paper ◽  
Fundamental Aspect ◽  
Membrane Domains ◽  
Polarized Cells ◽  
Plasma Membrane Domains ◽  
Polarized Epithelium

A fundamental aspect in the morphogenesis of a polarized epithelium is the formation of structurally and functionally distinct apical and basal-lateral domains of the plasma membrane. The formation of these membrane domains involves the accumulation of domain-specific proteins and removal of incorrectly localized proteins. The mechanisms involved in these processes are not well understood. We have approached this problem by detailed analysis of the distribution and fate of proteins specific for different membrane domains during reversal of epithelial polarity. In the preceding paper we showed that MDCK cells form multicellular cysts comprising a closed monolayer of polarized cells. The orientation of cell polarity depends upon whether cysts are formed in suspension culture or in a collagen gel. Here, we show that, when fully developed cysts formed in suspension culture are placed in a collagen gel, polarity is rapidly reversed without cell dissociation. We show that during the process of polarity reversal, plasma membrane domains are disassembled by uptake of proteins into cytoplasmic vesicles, followed by protein degradation that probably occurs in lysosomes. The disassembly and assembly of the apical and the basal-lateral membrane domains occur in a sequential order with different kinetics. Our results provide further insights into the establishment of protein specificity of plasma membrane domains in polarized cells.

scholarly journals Detergent Resistant Membrane Domains in Broccoli Plasma Membrane Associated to the Response to Salinity Stress

2020 ◽  
Vol 21 (20) ◽  
pp. 7694
Author(s):  
Lucía Yepes-Molina ◽  
Micaela Carvajal ◽  
Maria Carmen Martínez-Ballesta
Keyword(s):  
Plasma Membrane ◽  
Membrane Trafficking ◽  
Lower Amount ◽  
Membrane Domains ◽  
Cellular Functions ◽  
Osmotic Water ◽  
Fatty Acid Saturation ◽  
Protein Partitioning ◽  
Detergent Resistant Membranes ◽  
Detergent Resistant Membrane

Detergent-resistant membranes (DRMs) microdomains, or “raft lipids”, are key components of the plasma membrane (PM), being involved in membrane trafficking, signal transduction, cell wall metabolism or endocytosis. Proteins imbibed in these domains play important roles in these cellular functions, but there are few studies concerning DRMs under abiotic stress. In this work, we determine DRMs from the PM of broccoli roots, the lipid and protein content, the vesicles structure, their water osmotic permeability and a proteomic characterization focused mainly in aquaporin isoforms under salinity (80 mM NaCl). Based on biochemical lipid composition, higher fatty acid saturation and enriched sterol content under stress resulted in membranes, which decreased osmotic water permeability with regard to other PM vesicles, but this permeability was maintained under control and saline conditions; this maintenance may be related to a lower amount of total PIP1 and PIP2. Selective aquaporin isoforms related to the stress response such as PIP1;2 and PIP2;7 were found in DRMs and this protein partitioning may act as a mechanism to regulate aquaporins involved in the response to salt stress. Other proteins related to protein synthesis, metabolism and energy were identified in DRMs independently of the treatment, indicating their preference to organize in DMRs.

scholarly journals Polarized Sphingolipid Transport from the Subapical Compartment: Evidence for Distinct Sphingolipid Domains

1999 ◽  
Vol 10 (10) ◽  
pp. 3449-3461 ◽  
Author(s):  
Sven C. D. van IJzendoorn ◽  
Dick Hoekstra
Keyword(s):  
Plasma Membrane ◽  
Membrane Trafficking ◽  
Apical Membrane ◽  
Apical Plasma Membrane ◽  
Membrane Domains ◽  
Dibutyryl Camp ◽  
Calmodulin Antagonists ◽  
Luminal Side ◽  
Basolateral Plasma Membrane ◽  
Recycling Pathway

In polarized HepG2 cells, the sphingolipids glucosylceramide and sphingomyelin (SM), transported along the reverse transcytotic pathway, are sorted in subapical compartments (SACs), and subsequently targeted to either apical or basolateral plasma membrane domains, respectively. In the present study, evidence is provided that demonstrates that these sphingolipids constitute separate membrane domains at the luminal side of the SAC membrane. Furthermore, as revealed by the use of various modulators of membrane trafficking, such as calmodulin antagonists and dibutyryl-cAMP, it is shown that the fate of these separate sphingolipid domains is regulated by different signals, including those that govern cell polarity development. Thus under conditions that stimulate apical plasma membrane biogenesis, SM is rerouted from a SAC-to-basolateral to a SAC-to-apical pathway. The latter pathway represents the final leg in the transcytotic pathway, followed by the transcytotic pIgR–dIgA protein complex. Interestingly, this pathway is clearly different from the apical recycling pathway followed by glucosylceramide, further indicating that randomization of these pathways, which are both bound for the apical membrane, does not occur. The consequence of the potential coexistence of separate sphingolipid domains within the same compartment in terms of “raft” formation and apical targeting is discussed.

scholarly journals VANGL2 regulates membrane trafficking of MMP14 to control cell polarity and migration

Development ◽  
2012 ◽  
Vol 139 (14) ◽  
pp. e1-e1
Author(s):  
B. B. Williams ◽  
V. A. Cantrell ◽  
N. A. Mundell ◽  
A. C. Bennett ◽  
R. E. Quick ◽  
...  
Keyword(s):  
Cell Polarity ◽  
Membrane Trafficking ◽  
Control Cell ◽  
And Migration

scholarly journals A conserved signaling network monitors delivery of sphingolipids to the plasma membrane in budding yeast

2017 ◽  
Vol 28 (20) ◽  
pp. 2589-2599 ◽  
Author(s):  
Jesse Clarke ◽  
Noah Dephoure ◽  
Ira Horecka ◽  
Steven Gygi ◽  
Douglas Kellogg
Keyword(s):  
Cell Cycle ◽  
Plasma Membrane ◽  
Cell Growth ◽  
Membrane Trafficking ◽  
Ribosome Biogenesis ◽  
Essential Role ◽  
Budding Yeast ◽  
Control Cell ◽  
Signaling Network ◽  
Membrane Growth

In budding yeast, cell cycle progression and ribosome biogenesis are dependent on plasma membrane growth, which ensures that events of cell growth are coordinated with each other and with the cell cycle. However, the signals that link the cell cycle and ribosome biogenesis to membrane growth are poorly understood. Here we used proteome-wide mass spectrometry to systematically discover signals associated with membrane growth. The results suggest that membrane trafficking events required for membrane growth generate sphingolipid-dependent signals. A conserved signaling network appears to play an essential role in signaling by responding to delivery of sphingolipids to the plasma membrane. In addition, sphingolipid-dependent signals control phosphorylation of protein kinase C (Pkc1), which plays an essential role in the pathways that link the cell cycle and ribosome biogenesis to membrane growth. Together these discoveries provide new clues as to how growth-­dependent signals control cell growth and the cell cycle.

scholarly journals VANGL2 regulates membrane trafficking of MMP14 to control cell polarity and migration

2012 ◽  
Vol 125 (9) ◽  
pp. 2141-2147 ◽  
Author(s):  
B. B. Williams ◽  
V. A. Cantrell ◽  
N. A. Mundell ◽  
A. C. Bennett ◽  
R. E. Quick ◽  
...  
Keyword(s):  
Cell Polarity ◽  
Membrane Trafficking ◽  
Control Cell ◽  
And Migration

scholarly journals Fission yeast NDR/LATS kinase Orb6 regulates exocytosis via phosphorylation of exocyst complex

2018 ◽  
Author(s):  
Ye Dee Tay ◽  
Marcin Leda ◽  
Christos Spanos ◽  
Juri Rappsilber ◽  
Andrew B. Goryachev ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Cell Polarity ◽  
Membrane Trafficking ◽  
Critical Role ◽  
Control Cell ◽  
Small Gtpase ◽  
Nucleotide Exchange ◽  
Exocyst Complex ◽  
Growing Cell

ABSTRACTNDR/LATS kinases regulate multiple aspects of cell polarity and morphogenesis from yeast to mammals, but few of their substrates are known. Fission yeast NDR/LATS kinase Orb6 has been proposed to control cell polarity via spatial regulation of Gef1, a guanine nucleotide exchange factor for the small GTPase Cdc42. Here we show that Orb6 plays a critical role as a positive regulator of exocytosis, independent of Gef1. Through Orb6 inhibition in vivo and quantitative global phosphoproteomics, we identify several proteins involved in membrane trafficking as Orb6 targets, and we confirm Sec3 and Sec5, conserved components of the exocyst complex, as substrates of Orb6 both in vivo and in vitro. Our results suggest that Orb6 kinase activity is crucial for exocyst localization to actively-growing cell tips and for exocyst activity during septum dissolution after cytokinesis. We further show that Orb6 phosphorylation of Sec3 serine-201 contributes to exocyst function in parallel with exocyst protein Exo70. We propose that Orb6 contributes to polarized growth by regulating membrane trafficking at multiple levels.

scholarly journals Mechanistic Framework for Establishment, Maintenance, and Alteration of Cell Polarity in Plants

2012 ◽  
Vol 2012 ◽  
pp. 1-6 ◽  
Author(s):  
Pankaj Dhonukshe
Keyword(s):  
Plasma Membrane ◽  
Cell Polarity ◽  
Single Cells ◽  
Cell Types ◽  
Membrane Domains ◽  
Cell Transport ◽  
Agc Kinases ◽  
Polar Localization ◽  
Intact Plants ◽  
Polarity Establishment

Cell polarity establishment, maintenance, and alteration are central to the developmental and response programs of nearly all organisms and are often implicated in abnormalities ranging from patterning defects to cancer. By residing at the distinct plasma membrane domains polar cargoes mark the identities of those domains, and execute localized functions. Polar cargoes are recruited to the specialized membrane domains by directional secretion and/or directional endocytic recycling. In plants, auxin efflux carrier PIN proteins display polar localizations in various cell types and play major roles in directional cell-to-cell transport of signaling molecule auxin that is vital for plant patterning and response programs. Recent advanced microscopy studies applied to single cells in intact plants reveal subcellular PIN dynamics. They uncover the PIN polarity generation mechanism and identified important roles of AGC kinases for polar PIN localization. AGC kinase family members PINOID, WAG1, and WAG2, belonging to the AGC-3 subclass predominantly influence the polar localization of PINs. The emerging mechanism for AGC-3 kinases action suggests that kinases phosphorylate PINs mainly at the plasma membrane after initial symmetric PIN secretion for eventual PIN internalization and PIN sorting into distinct ARF-GEF-regulated polar recycling pathways. Thus phosphorylation status directs PIN translocation to different cell sides. Based on these findings a mechanistic framework evolves that suggests existence of cell side-specific recycling pathways in plants and implicates AGC3 kinases for differential PIN recruitment among them for eventual PIN polarity establishment, maintenance, and alteration.

scholarly journals A conserved signaling network monitors delivery of sphingolipids to the plasma membrane in budding yeast

2017 ◽  
Author(s):  
Jesse Clarke ◽  
Noah Dephoure ◽  
Ira Horecka ◽  
Steven Gygi ◽  
Douglas Kellogg
Keyword(s):  
Cell Cycle ◽  
Plasma Membrane ◽  
Cell Growth ◽  
Membrane Trafficking ◽  
Ribosome Biogenesis ◽  
Essential Role ◽  
Budding Yeast ◽  
Control Cell ◽  
Signaling Network ◽  
Membrane Growth

AbstractIn budding yeast, cell cycle progression and ribosome biogenesis are dependent upon plasma membrane growth, which ensures that events of cell growth are coordinated with each other and with the cell cycle. However, the signals that link the cell cycle and ribosome biogenesis to membrane growth are poorly understood. Here, we used proteome-wide mass spectrometry to systematically discover signals associated with membrane growth. The results suggest that membrane trafficking events required for membrane growth generate sphingolipid-dependent signals. A conserved signaling network plays an essential role in signaling by responding to delivery of sphingolipids to the plasma membrane. In addition, sphingolipid-dependent signals control phosphorylation of protein kinase C (Pkc1), which plays an essential role in the pathways that link the cell cycle and ribosome biogenesis to membrane growth. Together, these discoveries provide new clues to how growth-dependent signals control cell growth and the cell cycle.

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