scholarly journals Actin cytoskeleton self-organization in single epithelial cells and fibroblasts under isotropic confinement

2019 ◽  
Vol 132 (5) ◽  
pp. jcs220780 ◽  
Author(s):  
Salma Jalal ◽  
Shidong Shi ◽  
Vidhyalakshmi Acharya ◽  
Ruby Yun-Ju Huang ◽  
Virgile Viasnoff ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Actin Cytoskeleton ◽  
Self Organization

scholarly journals The Actin Cytoskeleton as a Barrier to Virus Infection of Polarized Epithelial Cells

Viruses ◽  
2011 ◽  
Vol 3 (12) ◽  
pp. 2462-2477 ◽  
Author(s):  
Elizabeth Delorme-Axford ◽  
Carolyn B. Coyne
Keyword(s):  
Epithelial Cells ◽  
Virus Infection ◽  
Actin Cytoskeleton ◽  
Polarized Epithelial Cells

scholarly journals Self-Organization and Force Production by the Branched Actin Cytoskeleton during Mammalian Clathrin-Mediated Endocytosis

2019 ◽  
Vol 116 (3) ◽  
pp. 313a ◽  
Author(s):  
Matthew Akamatsu ◽  
Ritvik Vasan ◽  
David G. Drubin ◽  
Daniel Serwas ◽  
Padmini Rangamani
Keyword(s):  
Actin Cytoskeleton ◽  
Force Production ◽  
Self Organization

Rho-kinase regulates myosin II activation in MDCK cells during recovery after ATP depletion

2001 ◽  
Vol 281 (5) ◽  
pp. F810-F818 ◽  
Author(s):  
Timothy A. Sutton ◽  
Henry E. Mang ◽  
Simon J. Atkinson
Keyword(s):  
Epithelial Cells ◽  
Actin Cytoskeleton ◽  
Mdck Cells ◽  
Myosin Ii ◽  
Atp Depletion ◽  
Stress Fibers ◽  
Tubular Epithelial Cells ◽  
Renal Tubular Epithelial Cells ◽  
Renal Tubular ◽  
Actin Stress Fibers

Alterations in the actin cytoskeleton of renal tubular epithelial cells during periods of ischemic injury and recovery have important consequences for normal cell and kidney function. Myosin II has been demonstrated to be an important effector in organizing basal actin structures in some cell types. ATP depletion in vitro has been demonstrated to recapitulate alterations of the actin cytoskeleton in renal tubular epithelial cells observed during renal ischemia in vivo. We utilized this reversible cell culture model of ischemia to examine the correlation of the activation state and cellular distribution of myosin II with disruption of actin stress fibers in Madin-Darby canine kidney (MDCK) cells during ATP depletion and recovery from ATP depletion. We found that myosin II inactivation occurs rapidly and precedes dissociation of myosin II from actin stress fibers during ATP depletion. Myosin II activation temporally correlates with colocalization of myosin II to reorganizing stress fibers during recovery from ATP depletion. Furthermore, myosin activation and actin stress fiber formation were found to be Rho-associated Ser/Thr protein kinase dependent during recovery from ATP depletion.

scholarly journals The type III TGFβ receptor regulates filopodia formation via a Cdc42-mediated IRSp53–N-WASP interaction in epithelial cells

2013 ◽  
Vol 454 (1) ◽  
pp. 79-89 ◽  
Author(s):  
Sun Young Oh ◽  
Erik H. Knelson ◽  
Gerard C. Blobe ◽  
Karthikeyan Mythreye
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Actin Cytoskeleton ◽  
Transforming Growth Factor ◽  
Small Gtpase ◽  
Mammary Epithelial ◽  
Migration And Invasion ◽  
Type Iii ◽  
Tgfβ Receptor

Cell adhesion and migration are tightly controlled by regulated changes in the actin cytoskeleton. Previously we reported that the TGFβ (transforming growth factor β) superfamily co-receptor, TβRIII (type III TGFβ receptor; also known as betaglycan), regulates cell adhesion, migration and invasion, and suppresses cancer progression, in part, through activation of the small GTPase Cdc42 (cell division cycle 42), and Cdc42-dependent alterations to the actin cytoskeleton. In the present study we demonstrate that TβRIII specifically promotes filopodial formation and extension in MCF10A and HMEC (human mammary epithelial cell) mammary epithelial cells. Mechanistically, cell-surface TβRIII and Cdc42 co-localize to filopodial structures and co-complex in a β-arrestin2-dependent, and a TβRI/TβRII-independent manner. The β-arrestin2-mediated interaction between TβRIII and Cdc42 increases complex formation between the Cdc42 effectors IRSp53 with N-WASP (neuronal Wiskott–Aldrich syndrome protein) to increase filopodial formation. We demonstrate a function link between filopodial structures and epithelial cell adhesion as regulated by the TβRIII–Cdc42 interaction. The present studies identify TβRIII as a novel regulator of IRSp53/N-WASP via Cdc42 to regulate filopodial formation and cell adhesion.

scholarly journals Interaction of microtubules with the actin cytoskeleton via cross-talk of EB1-containing +TIPs and γ-actin in epithelial cells

Oncotarget ◽  
2016 ◽  
Vol 7 (45) ◽  
pp. 72699-72715 ◽  
Author(s):  
Vera Dugina ◽  
Irina Alieva ◽  
Natalya Khromova ◽  
Igor Kireev ◽  
Peter W. Gunning ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Actin Cytoskeleton ◽  
Cross Talk
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