Visualization of Actin Cytoskeletal Dynamics in Fixed and Live Drosophila Egg Chambers

2015 ◽  
pp. 113-124 ◽  
Author(s):  
Christopher M. Groen ◽  
Tina L. Tootle
Keyword(s):  
Cytoskeletal Dynamics ◽  
Egg Chambers ◽  
Actin Cytoskeletal Dynamics

scholarly journals The localization and activity of sphingosine kinase 1 are coordinately regulated with actin cytoskeletal dynamics in macrophages. VOLUME 282 (2007) PAGES 23147-23162

2008 ◽  
Vol 283 (9) ◽  
pp. 5972
Author(s):  
David J. Kusner ◽  
Christopher R. Thompson ◽  
Natalie A. Melrose ◽  
Stuart M. Pitson ◽  
Lina M. Obeid ◽  
...  
Keyword(s):  
Sphingosine Kinase ◽  
Sphingosine Kinase 1 ◽  
Cytoskeletal Dynamics ◽  
Actin Cytoskeletal Dynamics

scholarly journals Bidirectional feedback between BCR signaling and actin cytoskeletal dynamics

FEBS Journal ◽  
2021 ◽  
Author(s):  
Anshuman Bhanja ◽  
Ivan Rey‐Suarez ◽  
Wenxia Song ◽  
Arpita Upadhyaya
Keyword(s):  
Bcr Signaling ◽  
Cytoskeletal Dynamics ◽  
Actin Cytoskeletal Dynamics

scholarly journals Role of Cyclic Nucleotide-Dependent Actin Cytoskeletal Dynamics: [Ca2+]i and Force Suppression in Forskolin-Pretreated Porcine Coronary Arteries

PLoS ONE ◽  
2013 ◽  
Vol 8 (4) ◽  
pp. e60986 ◽  
Author(s):  
Kyle M. Hocking ◽  
Franz J. Baudenbacher ◽  
Gowthami Putumbaka ◽  
Sneha Venkatraman ◽  
Joyce Cheung-Flynn ◽  
...  
Keyword(s):  
Coronary Arteries ◽  
Cyclic Nucleotide ◽  
Cytoskeletal Dynamics ◽  
Actin Cytoskeletal Dynamics

scholarly journals The Crystal Structure of Murine Coronin-1: A Regulator of Actin Cytoskeletal Dynamics in Lymphocytes

Structure ◽  
2006 ◽  
Vol 14 (1) ◽  
pp. 87-96 ◽  
Author(s):  
Brent A. Appleton ◽  
Ping Wu ◽  
Christian Wiesmann
Keyword(s):  
Crystal Structure ◽  
Cytoskeletal Dynamics ◽  
Actin Cytoskeletal Dynamics

scholarly journals Journey to the Center of the Cell: Cytoplasmic and Nuclear Actin in Immune Cell Functions

2021 ◽  
Vol 9 ◽  
Author(s):  
Julien Record ◽  
Mezida B. Saeed ◽  
Tomas Venit ◽  
Piergiorgio Percipalle ◽  
Lisa S. Westerberg
Keyword(s):  
Immune Cells ◽  
Immune Cell ◽  
Nuclear Actin ◽  
Actin Reorganization ◽  
Actin Remodeling ◽  
Cell Functions ◽  
Cytoplasmic Actin ◽  
Cytoskeletal Dynamics ◽  
Numerous Cell ◽  
Actin Cytoskeletal Dynamics

Actin cytoskeletal dynamics drive cellular shape changes, linking numerous cell functions to physiological and pathological cues. Mutations in actin regulators that are differentially expressed or enriched in immune cells cause severe human diseases known as primary immunodeficiencies underscoring the importance of efficienct actin remodeling in immune cell homeostasis. Here we discuss recent findings on how immune cells sense the mechanical properties of their environement. Moreover, while the organization and biochemical regulation of cytoplasmic actin have been extensively studied, nuclear actin reorganization is a rapidly emerging field that has only begun to be explored in immune cells. Based on the critical and multifaceted contributions of cytoplasmic actin in immune cell functionality, nuclear actin regulation is anticipated to have a large impact on our understanding of immune cell development and functionality.

scholarly journals PTEN dephosphorylates Abi1 to promote epithelial morphogenesis

2020 ◽  
Vol 219 (9) ◽  
Author(s):  
Yanmei Qi ◽  
Jie Liu ◽  
Joshua Chao ◽  
Peter A. Greer ◽  
Shaohua Li
Keyword(s):  
Phosphatase Activity ◽  
Pluripotent Stem Cells ◽  
Protein Phosphatase ◽  
Embryoid Bodies ◽  
Epithelial Morphogenesis ◽  
Homologous Protein ◽  
Lipid Phosphatase ◽  
Cytoskeletal Dynamics ◽  
Regulatory Complex ◽  
Actin Cytoskeletal Dynamics

The tumor suppressor PTEN is essential for early development. Its lipid phosphatase activity converts PIP3 to PIP2 and antagonizes the PI3K–Akt pathway. In this study, we demonstrate that PTEN’s protein phosphatase activity is required for epiblast epithelial differentiation and polarization. This is accomplished by reconstitution of PTEN-null embryoid bodies with PTEN mutants that lack only PTEN’s lipid phosphatase activity or both PTEN’s lipid and protein phosphatase activities. Phosphotyrosine antibody immunoprecipitation and mass spectrometry were used to identify Abi1, a core component of the WASP-family verprolin homologous protein (WAVE) regulatory complex (WRC), as a new PTEN substrate. We demonstrate that PTEN dephosphorylation of Abi1 at Y213 and S216 results in Abi1 degradation through the calpain pathway. This leads to down-regulation of the WRC and reorganization of the actin cytoskeleton. The latter is critical to the transformation of nonpolar pluripotent stem cells into the polarized epiblast epithelium. Our findings establish a link between PTEN and WAVE-Arp2/3–regulated actin cytoskeletal dynamics in epithelial morphogenesis.

scholarly journals α-Synuclein and Its A30P Mutant Affect Actin Cytoskeletal Structure and Dynamics

2009 ◽  
Vol 20 (16) ◽  
pp. 3725-3739 ◽  
Author(s):  
Vítor L. Sousa ◽  
Serena Bellani ◽  
Maila Giannandrea ◽  
Malikmohamed Yousuf ◽  
Flavia Valtorta ◽  
...  
Keyword(s):  
Hippocampal Neurons ◽  
Actin Polymerization ◽  
Wild Type ◽  
Cellular Processes ◽  
Cytoskeletal Dynamics ◽  
Endocytic Traffic ◽  
Actin Cytoskeletal Dynamics ◽  
Cytoskeletal Disruption ◽  
Familial Parkinson’S Disease ◽  
The Brain

The function of α-synuclein, a soluble protein abundant in the brain and concentrated at presynaptic terminals, is still undefined. Yet, α-synuclein overexpression and the expression of its A30P mutant are associated with familial Parkinson's disease. Working in cell-free conditions, in two cell lines as well as in primary neurons we demonstrate that α-synuclein and its A30P mutant have different effects on actin polymerization. Wild-type α-synuclein binds actin, slows down its polymerization and accelerates its depolymerization, probably by monomer sequestration; A30P mutant α-synuclein increases the rate of actin polymerization and disrupts the cytoskeleton during reassembly of actin filaments. Consequently, in cells expressing mutant α-synuclein, cytoskeleton-dependent processes, such as cell migration, are inhibited, while exo- and endocytic traffic is altered. In hippocampal neurons from mice carrying a deletion of the α-synuclein gene, electroporation of wild-type α-synuclein increases actin instability during remodeling, with growth of lamellipodia-like structures and apparent cell enlargement, whereas A30P α-synuclein induces discrete actin-rich foci during cytoskeleton reassembly. In conclusion, α-synuclein appears to play a major role in actin cytoskeletal dynamics and various aspects of microfilament function. Actin cytoskeletal disruption induced by the A30P mutant might alter various cellular processes and thereby play a role in the pathogenesis of neurodegeneration.

scholarly journals DrosophilaFascin is a novel downstream target of prostaglandin signaling during actin remodeling

2012 ◽  
Vol 23 (23) ◽  
pp. 4567-4578 ◽  
Author(s):  
Christopher M. Groen ◽  
Andrew J. Spracklen ◽  
Tiffany N. Fagan ◽  
Tina L. Tootle
Keyword(s):  
Nurse Cell ◽  
Mechanisms Of Action ◽  
Migration And Invasion ◽  
Cancer Cell Migration ◽  
Cortical Actin ◽  
Actin Remodeling ◽  
Downstream Target ◽  
Cytoskeletal Dynamics ◽  
Actin Cytoskeletal Dynamics ◽  
Filament Bundle

Although prostaglandins (PGs)—lipid signals produced downstream of cyclooxygenase (COX) enzymes—regulate actin cytoskeletal dynamics, their mechanisms of action are unknown. We previously established Drosophila oogenesis, in particular nurse cell dumping, as a new model to determine how PGs regulate actin remodeling. PGs, and thus the Drosophila COX-like enzyme Pxt, are required for both the parallel actin filament bundle formation and the cortical actin strengthening required for dumping. Here we provide the first link between Fascin (Drosophila Singed, Sn), an actin-bundling protein, and PGs. Loss of either pxt or fascin results in similar actin defects. Fascin interacts, both pharmacologically and genetically, with PGs, as reduced Fascin levels enhance the effects of COX inhibition and synergize with reduced Pxt levels to cause both parallel bundle and cortical actin defects. Conversely, overexpression of Fascin in the germline suppresses the effects of COX inhibition and genetic loss of Pxt. These data lead to the conclusion that PGs regulate Fascin to control actin remodeling. This novel interaction has implications beyond Drosophila, as both PGs and Fascin-1, in mammalian systems, contribute to cancer cell migration and invasion.

scholarly journals Integrin-Linked Kinase Regulates Process Extension in Oligodendrocytes via Control of Actin Cytoskeletal Dynamics

2013 ◽  
Vol 33 (23) ◽  
pp. 9781-9793 ◽  
Author(s):  
R. W. O'Meara ◽  
J.-P. Michalski ◽  
C. Anderson ◽  
K. Bhanot ◽  
P. Rippstein ◽  
...  
Keyword(s):  
Cytoskeletal Dynamics ◽  
Integrin Linked Kinase ◽  
Actin Cytoskeletal Dynamics
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