scholarly journals LINC complex independent perinuclear actin organization and cell migration

BIOCELL ◽  
2022 ◽  
Vol 46 (4) ◽  
pp. 931-935
Author(s):  
ANDREA FRACCHIA ◽  
GABI GERLITZ
Keyword(s):  
Cell Migration ◽  
Linc Complex ◽  
Actin Organization

scholarly journals Increased Lamin B1 Levels Promote Cell Migration by Altering Perinuclear Actin Organization

Cells ◽  
2020 ◽  
Vol 9 (10) ◽  
pp. 2161
Author(s):  
Andrea Fracchia ◽  
Tal Asraf ◽  
Mali Salmon-Divon ◽  
Gabi Gerlitz
Keyword(s):  
Cell Migration ◽  
Actin Filaments ◽  
Migration Rate ◽  
Tumor Formation ◽  
Cellular Migration ◽  
Lamin A ◽  
Linc Complex ◽  
Actin Organization ◽  
Lamin B1 ◽  
Promote Cell Migration

Cell migration requires reposition and reshaping of the cell nucleus. The nuclear lamina is highly important for migration of both primary and cancer cells. B-type lamins are important for proper migration of epicardial cells and neurons and increased lamin B to lamin A ratio accelerates cancer cell migration through confined spaces. Moreover, a positive association between lamin B1 levels and tumor formation and progression is found in various cancer types. Still, the molecular mechanism by which B-type lamins promote cell migration is not fully understood. To better understand this mechanism, we tested the effects of lamin B1 on perinuclear actin organization. Here we show that induction of melanoma cell migration leads to the formation of a cytosolic Linker of Nucleoskeleton and Cytoskeleton (LINC) complex-independent perinuclear actin rim, which has not been detected in migrating cells, yet. Significantly, increasing the levels of lamin B1 but not the levels of lamin A prevented perinuclear actin rim formation while accelerated the cellular migration rate. To interfere with the perinuclear actin rim, we generated a chimeric protein that is localized to the outer nuclear membrane and cleaves perinuclear actin filaments in a specific manner without disrupting other cytosolic actin filaments. Using this tool, we found that disruption of the perinuclear actin rim accelerated the cellular migration rate in a similar manner to lamin B1 over-expression. Taken together, our results suggest that increased lamin B1 levels can accelerate cell migration by inhibiting the association of the nuclear envelope with actin filaments that may reduce nuclear movement and deformability.

scholarly journals LINC complex-Lis1 interplay controls MT1-MMP matrix digest-on-demand response for confined tumor cell migration

2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Elvira Infante ◽  
Alessia Castagnino ◽  
Robin Ferrari ◽  
Pedro Monteiro ◽  
Sonia Agüera-González ◽  
...  
Keyword(s):  
Cell Migration ◽  
Tumor Cell ◽  
Demand Response ◽  
Linc Complex ◽  
Tumor Cell Migration ◽  
On Demand

Caldesmon affects actin organization at the leading edge and inhibits cell migration

BIOPHYSICS ◽  
2008 ◽  
Vol 53 (6) ◽  
pp. 527-532
Author(s):  
T. V. Kudryashova ◽  
P. N. Rutkevich ◽  
A. Ya. Shevelev ◽  
T. N. Vlasik ◽  
A. V. Vorotnikov
Keyword(s):  
Cell Migration ◽  
Leading Edge ◽  
Actin Organization

scholarly journals The Activity of Kv 11.1 Potassium Channel Modulates F-Actin Organization During Cell Migration of Pancreatic Ductal Adenocarcinoma Cells

Cancers ◽  
2019 ◽  
Vol 11 (2) ◽  
pp. 135 ◽  
Author(s):  
Sagar Manoli ◽  
Stefano Coppola ◽  
Claudia Duranti ◽  
Matteo Lulli ◽  
Lara Magni ◽  
...  
Keyword(s):  
Cell Migration ◽  
Potassium Channel ◽  
Pancreatic Ductal Adenocarcinoma ◽  
Actin Polymerization ◽  
Focal Adhesions ◽  
Stress Fibers ◽  
Pancreatic Stellate Cells ◽  
Ductal Adenocarcinoma ◽  
Actin Organization ◽  
Cells Cultured

Cell migration exerts a pivotal role in tumor progression, underlying cell invasion and metastatic spread. The cell migratory program requires f-actin re-organization, generally coordinated with the assembly of focal adhesions. Ion channels are emerging actors in regulating cell migration, through different mechanisms. We studied the role of the voltage dependent potassium channel KV 11.1 on cell migration of pancreatic ductal adenocarcinoma (PDAC) cells, focusing on its effects on f-actin organization and dynamics. Cells were cultured either on fibronectin (FN) or on a desmoplastic matrix (DM) with the addition of a conditioned medium produced by pancreatic stellate cells (PSC) maintained in hypoxia (Hypo-PSC-CM), to better mimic the PDAC microenvironment. KV11.1 was essential to maintain stress fibers in a less organized arrangement in cells cultured on FN. When PDAC cells were cultured on DM plus Hypo-PSC-CM, KV11.1 activity determined the organization of cortical f-actin into sparse and long filopodia, and allowed f-actin polymerization at a high speed. In both conditions, blocking KV11.1 impaired PDAC cell migration, and, on cells cultured onto FN, the effect was accompanied by a decrease of basal intracellular Ca2+ concentration. We conclude that KV11.1 is implicated in sustaining pro-metastatic signals in pancreatic cancer, through a reorganization of f-actin in stress fibers and a modulation of filopodia formation and dynamics.

scholarly journals Type I PIPK-α regulates directed cell migration by modulating Rac1 plasma membrane targeting and activation

2010 ◽  
Vol 190 (2) ◽  
pp. 247-262 ◽  
Author(s):  
Wei-Ting Chao ◽  
Alexes C. Daquinag ◽  
Felicity Ashcroft ◽  
Jeannette Kunz
Keyword(s):  
Plasma Membrane ◽  
Cell Migration ◽  
Adhesion Formation ◽  
Physical Interaction ◽  
Type I ◽  
Membrane Ruffling ◽  
Actin Organization ◽  
Upstream Regulator ◽  
Directed Cell Migration ◽  
Rac1 Activity

Phosphatidylinositol-4,5-bisphosphate (PI4,5P2) is a critical regulator of cell migration, but the roles of the type I phosphatidylinositol-4-phosphate 5-kinases (PIPKIs), which synthesize PI4,5P2, have yet to be fully defined in this process. In this study, we report that one kinase, PIPKI-α, is a novel upstream regulator of Rac1 that links activated integrins to the regulation of cell migration. We show that PIPKI-α controls integrin-induced translocation of Rac1 to the plasma membrane and thereby regulates Rac1 activation. Strikingly, this function is not shared with other PIPKI isoforms, is independent of catalytic activity, and requires physical interaction of PIPKI-α with the Rac1 polybasic domain. Consistent with its role in Rac1 activation, depletion of PIPKI-α causes pronounced defects in membrane ruffling, actin organization, and focal adhesion formation, and ultimately affects the directional persistence of migration. Thus, our study defines the role of PIPKI-α in cell migration and describes a new mechanism for the spatial regulation of Rac1 activity that is critical for cell migration.

Actin Organization and Cell Migration of Melanoma Cells Relate to Differential Expression of Integrins and Actin-associated Proteins

1992 ◽  
Vol 19 (11) ◽  
pp. 847-852 ◽  
Author(s):  
Hugh Randolph Byers ◽  
Takafumi Etoh† ◽  
Jacqueline Vink ◽  
Nancy Franklin ◽  
Sebastiano Gattoni-Celli ◽  
...  
Keyword(s):  
Cell Migration ◽  
Differential Expression ◽  
Melanoma Cells ◽  
Actin Organization ◽  
Associated Proteins

Role of the Crumbs proteins in ciliogenesis, cell migration and actin organization

2018 ◽  
Vol 81 ◽  
pp. 13-20 ◽  
Author(s):  
Elsa Bazellières ◽  
Veronika Aksenova ◽  
Magali Barthélémy-Requin ◽  
Dominique Massey-Harroche ◽  
André Le Bivic
Keyword(s):  
Cell Migration ◽  
Actin Organization

scholarly journals Zyxin Is Involved in Fibroblast Rigidity Sensing and Durotaxis

2021 ◽  
Vol 9 ◽  
Author(s):  
Ai Kia Yip ◽  
Songjing Zhang ◽  
Lor Huai Chong ◽  
Elsie Cheruba ◽  
Jessie Yong Xing Woon ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Migration ◽  
Actin Cytoskeleton ◽  
Focal Adhesions ◽  
Wild Type ◽  
Actin Organization ◽  
Rigidity Sensing ◽  
Substrate Rigidity ◽  
Cell Traction ◽  
Traction Stress

Focal adhesions (FAs) are specialized structures that enable cells to sense their extracellular matrix rigidity and transmit these signals to the interior of the cells, bringing about actin cytoskeleton reorganization, FA maturation, and cell migration. It is known that cells migrate towards regions of higher substrate rigidity, a phenomenon known as durotaxis. However, the underlying molecular mechanism of durotaxis and how different proteins in the FA are involved remain unclear. Zyxin is a component of the FA that has been implicated in connecting the actin cytoskeleton to the FA. We have found that knocking down zyxin impaired NIH3T3 fibroblast’s ability to sense and respond to changes in extracellular matrix in terms of their FA sizes, cell traction stress magnitudes and F-actin organization. Cell migration speed of zyxin knockdown fibroblasts was also independent of the underlying substrate rigidity, unlike wild type fibroblasts which migrated fastest at an intermediate substrate rigidity of 14 kPa. Wild type fibroblasts exhibited durotaxis by migrating toward regions of increasing substrate rigidity on polyacrylamide gels with substrate rigidity gradient, while zyxin knockdown fibroblasts did not exhibit durotaxis. Therefore, we propose zyxin as an essential protein that is required for rigidity sensing and durotaxis through modulating FA sizes, cell traction stress and F-actin organization.

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