scholarly journals Structural features and interfacial properties of WH2, β-thymosin domains and other intrinsically disordered domains in the regulation of actin cytoskeleton dynamics

Cytoskeleton ◽  
2013 ◽  
Vol 70 (11) ◽  
pp. 686-705 ◽  
Author(s):  
Louis Renault ◽  
Célia Deville ◽  
Carine van Heijenoort
Keyword(s):  
Actin Cytoskeleton ◽  
Interfacial Properties ◽  
Structural Features ◽  
Intrinsically Disordered ◽  
Cytoskeleton Dynamics ◽  
Regulation Of Actin Cytoskeleton

scholarly journals Rho Kinase‐mediated Regulation of Actin Cytoskeleton Dynamics Participates in NFATc3 Nuclear Transport

2011 ◽  
Vol 25 (S1) ◽  
Author(s):  
Juan Manuel Ramiro‐Diaz ◽  
Carlos Hiroshi Nitta ◽  
Mingma Sherpa ◽  
Laura Veronica Gonzalez Bosc
Keyword(s):  
Actin Cytoskeleton ◽  
Nuclear Transport ◽  
Rho Kinase ◽  
Cytoskeleton Dynamics ◽  
Regulation Of Actin Cytoskeleton

scholarly journals The PKGIα/VASP pathway is involved in insulin- and high glucose-dependent regulation of albumin permeability in cultured rat podocytes

2020 ◽  
Vol 168 (6) ◽  
pp. 575-588
Author(s):  
Patrycja Rachubik ◽  
Maria Szrejder ◽  
Irena Audzeyenka ◽  
Dorota Rogacka ◽  
Michał Rychłowski ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
High Glucose ◽  
Principal Component ◽  
Glomerular Permeability ◽  
Filtration Barrier ◽  
Vasp Phosphorylation ◽  
High Insulin ◽  
Cytoskeleton Dynamics ◽  
Regulation Of Actin Cytoskeleton

Abstract Podocytes, the principal component of the glomerular filtration barrier, regulate glomerular permeability to albumin via their contractile properties. Both insulin- and high glucose (HG)-dependent activation of protein kinase G type Iα (PKGIα) cause reorganization of the actin cytoskeleton and podocyte disruption. Vasodilator-stimulated phosphoprotein (VASP) is a substrate for PKGIα and involved in the regulation of actin cytoskeleton dynamics. We investigated the role of the PKGIα/VASP pathway in the regulation of podocyte permeability to albumin. We evaluated changes in high insulin- and/or HG-induced transepithelial albumin flux in cultured rat podocyte monolayers. Expression of PKGIα and downstream proteins was confirmed by western blot and immunofluorescence. We demonstrate that insulin and HG induce changes in the podocyte contractile apparatus via PKGIα-dependent regulation of the VASP phosphorylation state, increase VASP colocalization with PKGIα, and alter the subcellular localization of these proteins in podocytes. Moreover, VASP was implicated in the insulin- and HG-dependent dynamic remodelling of the actin cytoskeleton and, consequently, increased podocyte permeability to albumin under hyperinsulinaemic and hyperglycaemic conditions. These results indicate that insulin- and HG-dependent regulation of albumin permeability is mediated by the PKGIα/VASP pathway in cultured rat podocytes. This molecular mechanism may explain podocytopathy and albuminuria in diabetes.

scholarly journals Structural Aspects of LIMK Regulation and Pharmacology

Cells ◽  
2022 ◽  
Vol 11 (1) ◽  
pp. 142
Author(s):  
Deep Chatterjee ◽  
Franziska Preuss ◽  
Verena Dederer ◽  
Stefan Knapp ◽  
Sebastian Mathea
Keyword(s):  
Actin Cytoskeleton ◽  
Neurological Disorders ◽  
Catalytic Mechanism ◽  
Structural Features ◽  
Kinase Domain ◽  
Conformational Space ◽  
Lim Domain ◽  
Future Directions ◽  
Cytoskeleton Dynamics ◽  
Structural Aspects

Malfunction of the actin cytoskeleton is linked to numerous human diseases including neurological disorders and cancer. LIMK1 (LIM domain kinase 1) and its paralogue LIMK2 are two closely related kinases that control actin cytoskeleton dynamics. Consequently, they are potential therapeutic targets for the treatment of such diseases. In the present review, we describe the LIMK conformational space and its dependence on ligand binding. Furthermore, we explain the unique catalytic mechanism of the kinase, shedding light on substrate recognition and how LIMK activity is regulated. The structural features are evaluated for implications on the drug discovery process. Finally, potential future directions for targeting LIMKs pharmacologically, also beyond just inhibiting the kinase domain, are discussed.

scholarly journals Regulation of actin cytoskeleton dynamics in cells

2010 ◽  
Vol 29 (4) ◽  
pp. 311-325 ◽  
Author(s):  
Sung Haeng Lee ◽  
Roberto Dominguez
Keyword(s):  
Actin Cytoskeleton ◽  
Cytoskeleton Dynamics ◽  
Regulation Of Actin Cytoskeleton ◽  
In Cells

scholarly journals The insulin‐PI3K‐Rac1 axis contributes to terminal adipocyte differentiation through regulation of actin cytoskeleton dynamics

2020 ◽  
Vol 25 (3) ◽  
pp. 165-174
Author(s):  
Haruko Kunitomi ◽  
Yoshinao Oki ◽  
Nobuyuki Onishi ◽  
Koichiro Kano ◽  
Kouji Banno ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
Adipocyte Differentiation ◽  
Cytoskeleton Dynamics ◽  
Regulation Of Actin Cytoskeleton

Spatial control of actin-based motility through plasmalemmal PtdIns(4,5)P2-rich raft assemblies.

2005 ◽  
Vol 72 ◽  
pp. 119-127 ◽  
Author(s):  
Tamara Golub ◽  
Caroni Pico
Keyword(s):  
Protein Kinase ◽  
Cell Surface ◽  
Actin Cytoskeleton ◽  
Lipid Rafts ◽  
Patch Clustering ◽  
Pkc Protein Kinase C ◽  
Membrane Bound ◽  
And Function ◽  
Cytoskeleton Dynamics ◽  
Syndrome Protein

The interactions of cells with their environment involve regulated actin-based motility at defined positions along the cell surface. Sphingolipid- and cholesterol-dependent microdomains (rafts) order proteins at biological membranes, and have been implicated in most signalling processes at the cell surface. Many membrane-bound components that regulate actin cytoskeleton dynamics and cell-surface motility associate with PtdIns(4,5)P2-rich lipid rafts. Although raft integrity is not required for substrate-directed cell spreading, or to initiate signalling for motility, it is a prerequisite for sustained and organized motility. Plasmalemmal rafts redistribute rapidly in response to signals, triggering motility. This process involves the removal of rafts from sites that are not interacting with the substrate, apparently through endocytosis, and a local accumulation at sites of integrin-mediated substrate interactions. PtdIns(4,5)P2-rich lipid rafts can assemble into patches in a process depending on PtdIns(4,5)P2, Cdc42 (cell-division control 42), N-WASP (neural Wiskott-Aldrich syndrome protein) and actin cytoskeleton dynamics. The raft patches are sites of signal-induced actin assembly, and their accumulation locally promotes sustained motility. The patches capture microtubules, which promote patch clustering through PKA (protein kinase A), to steer motility. Raft accumulation at the cell surface, and its coupling to motility are influenced greatly by the expression of intrinsic raft-associated components that associate with the cytosolic leaflet of lipid rafts. Among them, GAP43 (growth-associated protein 43)-like proteins interact with PtdIns(4,5)P2 in a Ca2+/calmodulin and PKC (protein kinase C)-regulated manner, and function as intrinsic determinants of motility and anatomical plasticity. Plasmalemmal PtdIns(4,5)P2-rich raft assemblies thus provide powerful organizational principles for tight spatial and temporal control of signalling in motility.

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