scholarly journals The mechanosensitive Piezo1 channel controls endosome trafficking for an efficient cytokinetic abscission

2021 ◽  
Vol 7 (44) ◽  
Author(s):  
Julia Carrillo-Garcia ◽  
Víctor Herrera-Fernández ◽  
Selma A. Serra ◽  
Fanny Rubio-Moscardo ◽  
Marina Vogel-Gonzalez ◽  
...  
Keyword(s):  
Endosome Trafficking

Modulation of RAB5A early endosome trafficking in response to KRas mediated macropinocytic fluxes in pancreatic cancer cells

2017 ◽  
Vol 493 (1) ◽  
pp. 528-533 ◽  
Author(s):  
Christian Teske ◽  
Christine Schweitzer ◽  
Andrea Palamidessi ◽  
Daniela E. Aust ◽  
Giorgio Scita ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Cancer Cells ◽  
Early Endosome ◽  
Endosome Trafficking ◽  
Pancreatic Cancer Cells

scholarly journals IL-1β impairs retrograde flow of BDNF signaling by attenuating endosome trafficking

2017 ◽  
Vol 14 (1) ◽  
Author(s):  
Anthony J. Carlos ◽  
Liqi Tong ◽  
G. Aleph Prieto ◽  
Carl W. Cotman
Keyword(s):  
Retrograde Flow ◽  
Endosome Trafficking ◽  
Bdnf Signaling

scholarly journals Als2-deficient mice exhibit disturbances in endosome trafficking associated with motor behavioral abnormalities

2006 ◽  
Vol 103 (25) ◽  
pp. 9595-9600 ◽  
Author(s):  
R. S. Devon ◽  
P. C. Orban ◽  
K. Gerrow ◽  
M. A. Barbieri ◽  
C. Schwab ◽  
...  
Keyword(s):  
Endosome Trafficking ◽  
Behavioral Abnormalities ◽  
Deficient Mice

Detection of ClC-3 and ClC-5 in epididymal epithelium: immunofluorescence and RT-PCR after LCM

2003 ◽  
Vol 284 (1) ◽  
pp. C220-C232 ◽  
Author(s):  
Corinne Isnard-Bagnis ◽  
Nicolas Da Silva ◽  
Valérie Beaulieu ◽  
Alan S. L. Yu ◽  
Dennis Brown ◽  
...  
Keyword(s):  
Vas Deferens ◽  
Chloride Transport ◽  
The Body ◽  
Transepithelial Transport ◽  
Rt Pcr ◽  
Clear Cells ◽  
Principal Cells ◽  
Endosome Trafficking ◽  
Cauda Epididymidis ◽  
Laser Capture

Epithelial cells of the epididymis and vas deferens establish an optimum luminal environment in which spermatozoa mature and are stored. This is achieved by active transepithelial transport of various ions including Cl−and H+. We investigated the localization of three closely related members of the ClC family, ClC-3, ClC-4, and ClC-5, in the epididymis and vas deferens. RT-PCR using mRNA isolated by laser capture microdissection (LCM)-detected ClC-3 and ClC-5 transcripts but did not detect any ClC-4-specific transcript. Western blot and immunofluorescence analysis demonstrated that ClC-3 and ClC-5 proteins are present in all regions of the epididymis and in the vas deferens. ClC-5 is expressed exclusively in H+-ATPase-rich cells (narrow and clear cells). Confocal microscopy showed that ClC-5 partially colocalizes with the H+-ATPase in the subapical pole of clear cells. ClC-3 is strongly expressed in the apical membrane of principal cells of the caput epididymidis and the vas deferens and is less abundant in principal cells of the body and cauda epididymidis. These findings are consistent with a potential role for ClC-3 in transepithelial chloride transport by principal cells and for ClC-5 in the acidification of H+-ATPase-containing vesicles in narrow and clear cells. ClC-5 might facilitate endosome trafficking in the epididymis, as has been proposed in the kidney.

scholarly journals The schizophrenia susceptibility factor dysbindin and its associated complex sort cargoes from cell bodies to the synapse

2011 ◽  
Vol 22 (24) ◽  
pp. 4854-4867 ◽  
Author(s):  
Jennifer Larimore ◽  
Karine Tornieri ◽  
Pearl V. Ryder ◽  
Avanti Gokhale ◽  
Stephanie A. Zlatic ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Cortical Neurons ◽  
Neuronal Cells ◽  
Neuronal Cell ◽  
Adaptor Protein ◽  
Nerve Terminals ◽  
Endosome Trafficking ◽  
Neuronal Cell Bodies ◽  
Cultured Cortical Neurons ◽  
Lysosome Related Organelles

Dysbindin assembles into the biogenesis of lysosome-related organelles complex 1 (BLOC-1), which interacts with the adaptor protein complex 3 (AP-3), mediating a common endosome-trafficking route. Deficiencies in AP-3 and BLOC-1 affect synaptic vesicle composition. However, whether AP-3-BLOC-1–dependent sorting events that control synapse membrane protein content take place in cell bodies upstream of nerve terminals remains unknown. We tested this hypothesis by analyzing the targeting of phosphatidylinositol-4-kinase type II α (PI4KIIα), a membrane protein present in presynaptic and postsynaptic compartments. PI4KIIα copurified with BLOC-1 and AP-3 in neuronal cells. These interactions translated into a decreased PI4KIIα content in the dentate gyrus of dysbindin-null BLOC-1 deficiency and AP-3–null mice. Reduction of PI4KIIα in the dentate reflects a failure to traffic from the cell body. PI4KIIα was targeted to processes in wild-type primary cultured cortical neurons and PC12 cells but failed to reach neurites in cells lacking either AP-3 or BLOC-1. Similarly, disruption of an AP-3–sorting motif in PI4KIIα impaired its sorting into processes of PC12 and primary cultured cortical neuronal cells. Our findings indicate a novel vesicle transport mechanism requiring BLOC-1 and AP-3 complexes for cargo sorting from neuronal cell bodies to neurites and nerve terminals.

scholarly journals Nitric oxide may regulate focal adhesion turnover and cell migration in MDA-MB-231 breast cancer cells by modulating early endosome trafficking

2021 ◽  
Vol 9 (2) ◽  
pp. 60-72
Author(s):  
Dhurgham Al-Fahad ◽  
Bandar Fahad Alharbi ◽  
Clementino Ibeas Bih ◽  
Philip Richard Dash
Keyword(s):  
Breast Cancer ◽  
Nitric Oxide ◽  
Cell Migration ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Focal Adhesions ◽  
Early Endosome ◽  
No Synthase ◽  
Endosome Trafficking ◽  
In Cells

Abstract Cell migration is an essential process for wound healing, metastasis and inflammation. Focal adhesions (FA) are local regions of plasma membrane consisting of multiprotein complexes providing adhesive contact between the cell and the extracellular matrix (ECM). FA turnover regulates different signalling pathways implicated in various cellular responses (e.g. cell migration). Endocytosis, specifically the dynamin and clathrin pathways, is known to regulate cell migration by modulating FA dynamics. In this study, we investigated whether NO activity regulates cell migration, FA dynamics and early endosome trafficking in MDA-MB-231 cells. The assessment of cell migration showed a slowing down of cell migration and an increased duration of FA turnover in cells treated with inhibitors of NO synthase (NOS) such as L-NAME or 1400W. In addition, these treatments were found to exhibit no effect on transferrin and dextran uptake mediated by endocytosis and micropinocytosis, respectively. The number of early endosome antigen 1 (EEA1)-positive endosomes was reduced while their sizes were found to increase in cells treated with L-NAME or 1400W. In contrast, these inhibitors did not affect the number nor the size of Rab5-positive endosomes. Furthermore, we demonstrated that EEA1, endothelial NO synthase (eNOS) and inducible NO synthase (iNOS) were colocalised. Using the biotin switch assay followed by western blot, we showed that early endosome proteins such as APPL1, EEA1, Rab5 were found to be S-nitrosylated. These results were further supported by the sequence analysis performed with the GPS-SNO algorithm which predicted the S-nitrosylation of these endosomal proteins. Taken together, our findings suggest that NO might be involved in cell migration and FA turnover through early endosome trafficking in MDA-MB-231 cells. Running title: Nitric oxide in MDA-MB-231 breast cancer cells

Virus-Induced Signaling Influences Endosome Trafficking, Virus Entry, and Replication

2014 ◽  
pp. 65-76
Author(s):  
David J. Marchant ◽  
Leanne Bilawchuk ◽  
Gordon Nish ◽  
Richard G. Hegele
Keyword(s):  
Virus Entry ◽  
Endosome Trafficking

scholarly journals PAK Kinases Target Sortilin and Modulate Its Sorting

2019 ◽  
Vol 40 (3) ◽  
Author(s):  
Lone Tjener Pallesen ◽  
Camilla Gustafsen ◽  
Jacob Flyvholm Cramer ◽  
Steen Vang Petersen ◽  
Søren Skou Thirup ◽  
...  
Keyword(s):  
Rho Gtpases ◽  
Intracellular Transport ◽  
Intracellular Localization ◽  
Adaptor Proteins ◽  
Serine Residue ◽  
Endosome Trafficking ◽  
Downstream Effectors ◽  
Dileucine Motif ◽  
Group A ◽  
Kinase Phosphorylation

ABSTRACT The multifunctional type 1 receptor sortilin is involved in endocytosis and intracellular transport of ligands. The short intracellular domain of sortilin binds several cytoplasmic adaptor proteins (e.g., the AP-1 complex and GGA1 to -3), most of which target two well-defined motifs: a C-terminal acidic cluster dileucine motif and a YXXΦ motif in the proximal third of the domain. Both motifs contribute to endocytosis as well as Golgi-endosome trafficking of sortilin. The C-terminal acidic cluster harbors a serine residue, which is subject to phosphorylation by casein kinase. Phosphorylation of this serine residue is known to modulate adaptor binding to sortilin. Here, we show that the cytoplasmic domain of sortilin also engages Rac-p21-activated kinases 1 to 3 (PAK1-3) via a binding segment that includes a tyrosine-based motif, also encompassing a serine residue. We further demonstrate that PAK1-3 specifically phosphorylate this serine residue and that this phosphorylation alters the affinity for AP-1 binding and consequently changes the intracellular localization of sortilin as a result of modulated trafficking. Our findings suggest that trafficking of ligands bound to sortilin is in part regulated by group A PAK kinases, which are downstream effectors of Rho GTPases and are known to affect a variety of processes by remodeling the cytoskeleton and by promoting gene transcription and cell survival.

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