Vps1, a recycling factor for the traffic from early endosome to the late Golgi

2013 ◽  
Vol 91 (6) ◽  
pp. 455-465 ◽  
Author(s):  
Joshua Lukehart ◽  
Chad Highfill ◽  
Kyoungtae Kim
Keyword(s):  
Cell Survival ◽  
Budding Yeast ◽  
Membrane Traffic ◽  
Early Endosome ◽  
Genetic Interactions ◽  
Cellular Membranes ◽  
Early Endosomes ◽  
Survival And Growth ◽  
Mild Defect ◽  
Actin Cables

Recycling of cellular membranes and their constituents plays a role for cell survival and growth. In the budding yeast, there are recycling traffics from early and late endosomal compartments to the late Golgi. Here, we examined a possible role for Vps1, a large GTPase, in the recycling traffic of GFP-Snc1 from early endosomes to the late Golgi. In the absence of Vps1 we observed an aberrant accumulation of GFP-Snc1 puncta in the cytoplasm that we identified as early endosomes. The N-terminal GTPase and the C-terminal GED domains of Vps1 are essential for Vps1’s function in Snc1 recycling. Our finding of genetic interactions of VPS1 with genes involved in early endosome-to-Golgi traffic further suggests Vps1 functions as a recycling factor in the membrane traffic. Finally, we provide evidence that the severe accumulation of GFP-Snc1 cytoplasmic puncta in vps1Δ cells is attributed to a mild defect in the retention of the GARP component Vps51 at the late Golgi, as well as a severe disruption of actin cables.

Membrane traffic related to endosome dynamics and protein secretion in filamentous fungi

2021 ◽  
Author(s):  
Yujiro Higuchi
Keyword(s):  
Filamentous Fungi ◽  
Protein Secretion ◽  
Secretory Pathway ◽  
Molecular Mechanisms ◽  
Membrane Traffic ◽  
Early Endosome ◽  
Protein Glycosylation ◽  
Hyphal Cell ◽  
Cell Factories ◽  
Membrane Contacts

ABSTRACT In eukaryotic cells, membrane-surrounded organelles are orchestrally organized spatiotemporally under environmental situations. Among such organelles, vesicular transports and membrane contacts occur to communicate each other, so-called membrane traffic. Filamentous fungal cells are highly polarized and thus membrane traffic is developed to have versatile functions. Early endosome (EE) is an endocytic organelle that dynamically exhibits constant long-range motility through the hyphal cell, which is proven to have physiological roles, such as other organelle distribution and signal transduction. Since filamentous fungal cells are also considered as cell factories, to produce valuable proteins extracellularly, molecular mechanisms of secretory pathway including protein glycosylation have been well investigated. In this review, molecular and physiological aspects of membrane traffic especially related to EE dynamics and protein secretion in filamentous fungi are summarized, and perspectives for application are also described.

The enhancement of neural stem cell survival and growth by coculturing with expanded sertoli cells in vitro

2011 ◽  
Vol 28 (1) ◽  
pp. 196-205 ◽  
Author(s):  
Bingyang Shi ◽  
Lei Deng ◽  
Xiaolin Shi ◽  
Sheng Dai ◽  
Hu Zhang ◽  
...  
Keyword(s):  
Stem Cell ◽  
Cell Survival ◽  
Neural Stem Cell ◽  
Sertoli Cells ◽  
Stem Cell Survival ◽  
Survival And Growth

scholarly journals PAS Kinase Promotes Cell Survival and Growth Through Activation of Rho1

2012 ◽  
Vol 5 (209) ◽  
pp. ra9-ra9 ◽  
Author(s):  
C. M. Cardon ◽  
T. Beck ◽  
M. N. Hall ◽  
J. Rutter
Keyword(s):  
Cell Survival ◽  
Pas Kinase ◽  
Survival And Growth

scholarly journals Peroxisomes move by hitchhiking on early endosomes using the novel linker protein PxdA

2015 ◽  
Author(s):  
John Salogiannis ◽  
Martin J. Egan ◽  
Samara L. Reck-Peterson
Keyword(s):  
Molecular Motors ◽  
Intracellular Transport ◽  
Coiled Coil ◽  
Leading Edge ◽  
Time Lapse ◽  
Early Endosome ◽  
Organelle Transport ◽  
The Novel ◽  
Coiled Coil Region ◽  
Early Endosomes

Eukaryotic cells use microtubule-based intracellular transport for the delivery of many subcellular cargos, including organelles. The canonical view of organelle transport is that organelles directly recruit molecular motors via cargo-specific adaptors. In contrast to this view, we show here that peroxisomes move by hitchhiking on early endosomes, an organelle that directly recruits the transport machinery. Using the filamentous fungus Aspergillus nidulans we find that hitchhiking is mediated by a novel endosome-associated linker protein, PxdA. PxdA is required for normal distribution and long-range movement of peroxisomes, but not early endosomes or nuclei. Using simultaneous time-lapse imaging we find that early endosome-associated PxdA localizes to the leading edge of moving peroxisomes. We identify a coiled-coil region within PxdA that is necessary and sufficient for early endosome localization and peroxisome distribution and motility. These results present a new mechanism of microtubule-based organelle transport where peroxisomes hitchhike on early endosomes and identify PxdA as the novel linker protein required for this coupling.

scholarly journals Arp2/3 mediates early endosome dynamics necessary for the maintenance of PAR asymmetry in Caenorhabditis elegans

2012 ◽  
Vol 23 (10) ◽  
pp. 1917-1927 ◽  
Author(s):  
Jessica M. Shivas ◽  
Ahna R. Skop
Keyword(s):  
Caenorhabditis Elegans ◽  
Maintenance Phase ◽  
Early Endosome ◽  
Actin Dynamics ◽  
Cellular Polarity ◽  
Cortical Actin ◽  
Endocytic Recycling ◽  
C Elegans ◽  
Early Endosomes ◽  
Stable Maintenance

The widely conserved Arp2/3 complex regulates branched actin dynamics that are necessary for a variety of cellular processes. In Caenorhabditis elegans, the actin cytoskeleton has been extensively characterized in its role in establishing PAR asymmetry; however, the contributions of actin to the maintenance of polarity before the onset of mitosis are less clear. Endocytic recycling has emerged as a key mechanism in the dynamic stabilization of cellular polarity, and the large GTPase dynamin participates in the stabilization of cortical polarity during maintenance phase via endocytosis in C. elegans. Here we show that disruption of Arp2/3 function affects the formation and localization of short cortical actin filaments and foci, endocytic regulators, and polarity proteins during maintenance phase. We detect actin associated with events similar to early endosomal fission, movement of endosomes into the cytoplasm, and endosomal movement from the cytoplasm to the plasma membrane, suggesting the involvement of actin in regulating processes at the early endosome. We also observe aberrant accumulations of PAR-6 cytoplasmic puncta near the centrosome along with early endosomes. We propose a model in which Arp2/3 affects the efficiency of rapid endocytic recycling of polarity cues that ultimately contributes to their stable maintenance.

scholarly journals Targeting PRMT1-mediated FLT3 methylation disrupts maintenance of MLL-rearranged acute lymphoblastic leukemia

Blood ◽  
2019 ◽  
Vol 134 (15) ◽  
pp. 1257-1268 ◽  
Author(s):  
Yinghui Zhu ◽  
Xin He ◽  
Yi-Chun Lin ◽  
Haojie Dong ◽  
Lei Zhang ◽  
...  
Keyword(s):  
Acute Lymphoblastic Leukemia ◽  
Tyrosine Kinase ◽  
Cell Survival ◽  
Tyrosine Kinase Inhibitor ◽  
Kinase Inhibitor ◽  
Lymphoblastic Leukemia ◽  
Key Points ◽  
Survival And Growth ◽  
Inhibitor Treatment

Key Points High PRMT1 expression maintains MLL-r ALL cell survival and growth by regulating FLT3 methylation at R972/973. PRMT1 inhibition enhances ablation of MLL-r ALL by tyrosine kinase inhibitor treatment.

scholarly journals TRIM25 promotes the cell survival and growth of hepatocellular carcinoma through targeting Keap1-Nrf2 pathway

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Yanfeng Liu ◽  
Shishi Tao ◽  
Lijuan Liao ◽  
Yang Li ◽  
Hongchang Li ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Cell Survival ◽  
Nrf2 Pathway ◽  
Survival And Growth

scholarly journals Rabenosyn-5, a Novel Rab5 Effector, Is Complexed with Hvps45 and Recruited to Endosomes through a Fyve Finger Domain

2000 ◽  
Vol 151 (3) ◽  
pp. 601-612 ◽  
Author(s):  
Erik Nielsen ◽  
Savvas Christoforidis ◽  
Sandrine Uttenweiler-Joseph ◽  
Marta Miaczynska ◽  
Frederique Dewitte ◽  
...  
Keyword(s):  
Early Endosome ◽  
Effector Proteins ◽  
Endosomal Trafficking ◽  
Membrane Domains ◽  
Phosphatidylinositol 3 Kinase ◽  
Early Endosomes ◽  
Site Of Action ◽  
Endosomal Membranes ◽  
Novel Protein ◽  
Phosphatidylinositol 3

Rab5 regulates endocytic membrane traffic by specifically recruiting cytosolic effector proteins to their site of action on early endosomal membranes. We have characterized a new Rab5 effector complex involved in endosomal fusion events. This complex includes a novel protein, Rabenosyn-5, which, like the previously characterized Rab5 effector early endosome antigen 1 (EEA1), contains an FYVE finger domain and is recruited in a phosphatidylinositol-3-kinase–dependent fashion to early endosomes. Rabenosyn-5 is complexed to the Sec1-like protein hVPS45. hVPS45 does not interact directly with Rab5, therefore Rabenosyn-5 serves as a molecular link between hVPS45 and the Rab5 GTPase. This property suggests that Rabenosyn-5 is a closer mammalian functional homologue of yeast Vac1p than EEA1. Furthermore, although both EEA1 and Rabenosyn-5 are required for early endosomal fusion, only overexpression of Rabenosyn-5 inhibits cathepsin D processing, suggesting that the two proteins play distinct roles in endosomal trafficking. We propose that Rab5-dependent formation of membrane domains enriched in phosphatidylinositol-3-phosphate has evolved as a mechanism for the recruitment of multiple effector proteins to mammalian early endosomes, and that these domains are multifunctional, depending on the differing activities of the effector proteins recruited.

scholarly journals Myo6 Facilitates the Translocation of Endocytic Vesicles from Cell Peripheries

2003 ◽  
Vol 14 (7) ◽  
pp. 2728-2743 ◽  
Author(s):  
Laura Aschenbrenner ◽  
TinThu Lee ◽  
Tama Hasson
Keyword(s):  
Epithelial Cells ◽  
Fluorescent Protein ◽  
Early Endosome ◽  
Sufficient Time ◽  
Significant Delay ◽  
Transfected Cells ◽  
Early Endosomes ◽  
Green Fluorescent ◽  
Endocytic Vesicles ◽  
Transferrin Uptake

Immunolocalization studies in epithelial cells revealed myo6 was associated with peripherally located vesicles that contained the transferrin receptor. Pulse-chase experiments after transferrin uptake showed that these vesicles were newly uncoated endocytic vesicles and that myo6 was recruited to these vesicles immediately after uncoating. GIPC, a putative myo6 tail binding protein, was also present. Myo6 was not present on early endosomes, suggesting that myo6 has a transient association with endocytic vesicles and is released upon early endosome fusion. Green fluorescent protein (GFP) fused to myo6 as well as the cargo-binding tail (M6tail) alone targeted to the nascent endocytic vesicles. Overexpression of GFP-M6tail had no effect on a variety of organelle markers; however, GFP-M6tail displaced the endogenous myo6 from nascent vesicles and resulted in a significant delay in transferrin uptake. Pulse-chase experiments revealed that transferrin accumulated in uncoated vesicles within the peripheries of transfected cells and that Rab5 was recruited to the surface of these vesicles. Given sufficient time, the transferrin did traffic to the perinuclear sorting endosome. These data suggest that myo6 is an accessory protein required for the efficient transportation of nascent endocytic vesicles from the actin-rich peripheries of epithelial cells, allowing for timely fusion of endocytic vesicles with the early endosome.

scholarly journals The p25 subunit of the dynactin complex is required for dynein–early endosome interaction

2011 ◽  
Vol 193 (7) ◽  
pp. 1245-1255 ◽  
Author(s):  
Jun Zhang ◽  
Xuanli Yao ◽  
Lauren Fischer ◽  
Juan F. Abenza ◽  
Miguel A. Peñalva ◽  
...  
Keyword(s):  
Aspergillus Nidulans ◽  
Cytoplasmic Dynein ◽  
Early Endosome ◽  
Physical Interaction ◽  
Nuclear Distribution ◽  
Early Endosomes ◽  
Pointed End ◽  
Dynactin Complex ◽  
Hyphal Tip

Cytoplasmic dynein transports various cellular cargoes including early endosomes, but how dynein is linked to early endosomes is unclear. We find that the Aspergillus nidulans orthologue of the p25 subunit of dynactin is critical for dynein-mediated early endosome movement but not for dynein-mediated nuclear distribution. In the absence of NUDF/LIS1, p25 deletion abolished the localization of dynein–dynactin to the hyphal tip where early endosomes abnormally accumulate but did not prevent dynein–dynactin localization to microtubule plus ends. Within the dynactin complex, p25 locates at the pointed end of the Arp1 filament with Arp11 and p62, and our data suggest that Arp11 but not p62 is important for p25–dynactin association. Loss of either Arp1 or p25 significantly weakened the physical interaction between dynein and early endosomes, although loss of p25 did not apparently affect the integrity of the Arp1 filament. These results indicate that p25, in conjunction with the rest of the dynactin complex, is important for dynein–early endosome interaction.

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