Nonmuscle Myosin II Regulation Directs Its Multiple Roles in Cell Migration and Division

2021 ◽  
Vol 37 (1) ◽  
Author(s):  
Marina Garrido-Casado ◽  
Gloria Asensio-Juárez ◽  
Miguel Vicente-Manzanares
Keyword(s):  
Cell Migration ◽  
Conformational Changes ◽  
Myosin Ii ◽  
Annual Review ◽  
Publication Date ◽  
Dependent Manner ◽  
Control Force ◽  
Nonmuscle Myosin ◽  
Nonmuscle Myosin Ii ◽  
The Stability

Nonmuscle myosin II (NMII) is a multimeric protein complex that generates most mechanical force in eukaryotic cells. NMII function is controlled at three main levels. The first level includes events that trigger conformational changes that extend the complex to enable its assembly into filaments. The second level controls the ATPase activity of the complex and its binding to microfilaments in extended NMII filaments. The third level includes events that modulate the stability and contractility of the filaments. They all work in concert to finely control force generation inside cells. NMII is a common endpoint of mechanochemical signaling pathways that control cellular responses to physical and chemical extracellular cues. Specific phosphorylations modulate NMII activation in a context-dependent manner. A few kinases control these phosphorylations in a spatially, temporally, and lineage-restricted fashion, enabling functional adaptability to the cellular microenvironment. Here, we review mechanisms that control NMII activity in the context of cell migration and division. Expected final online publication date for the Annual Review of Cell and Developmental Biology, Volume 37 is October 2021. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

scholarly journals LIMCH1 regulates nonmuscle myosin-II activity and suppresses cell migration

2017 ◽  
Vol 28 (8) ◽  
pp. 1054-1065 ◽  
Author(s):  
Yu-Hung Lin ◽  
Yen-Yi Zhen ◽  
Kun-Yi Chien ◽  
I-Ching Lee ◽  
Wei-Chi Lin ◽  
...  
Keyword(s):  
Cell Migration ◽  
Hela Cells ◽  
Myosin Ii ◽  
Focal Adhesions ◽  
Stress Fiber ◽  
Stress Fibers ◽  
Actin Stress Fiber ◽  
Nonmuscle Myosin ◽  
Head Region ◽  
Nonmuscle Myosin Ii

Nonmuscle myosin II (NM-II) is an important motor protein involved in cell migration. Incorporation of NM-II into actin stress fiber provides a traction force to promote actin retrograde flow and focal adhesion assembly. However, the components involved in regulation of NM-II activity are not well understood. Here we identified a novel actin stress fiber–associated protein, LIM and calponin-homology domains 1 (LIMCH1), which regulates NM-II activity. The recruitment of LIMCH1 into contractile stress fibers revealed its localization complementary to actinin-1. LIMCH1 interacted with NM-IIA, but not NM-IIB, independent of the inhibition of myosin ATPase activity with blebbistatin. Moreover, the N-terminus of LIMCH1 binds to the head region of NM-IIA. Depletion of LIMCH1 attenuated myosin regulatory light chain (MRLC) diphosphorylation in HeLa cells, which was restored by reexpression of small interfering RNA–resistant LIMCH1. In addition, LIMCH1-depleted HeLa cells exhibited a decrease in the number of actin stress fibers and focal adhesions, leading to enhanced cell migration. Collectively, our data suggest that LIMCH1 plays a positive role in regulation of NM-II activity through effects on MRLC during cell migration.

Role of nonmuscle myosin II in polyamine-dependent intestinal epithelial cell migration

1996 ◽  
Vol 270 (2) ◽  
pp. G355-G362 ◽  
Author(s):  
J. Y. Wang ◽  
S. A. McCormack ◽  
L. R. Johnson
Keyword(s):  
Cell Migration ◽  
Myosin Ii ◽  
Specific Inhibitor ◽  
Intestinal Epithelial ◽  
Nonmuscle Myosin ◽  
Nonmuscle Myosin Ii ◽  
Epithelial Cell Migration ◽  
Vitro Model

The current study determines whether nonmuscle myosin II is involved in the process requiring polyamines for the stimulation of cell migration in an in vitro model that mimics the early stages of epithelial restitution. Treatment with alpha-difluoromethylornithine (DFMO), a specific inhibitor of ornithine decarboxylase (ODC), for 4 days totally inhibited ODC activity and depleted intracellular polyamines in the IEC-6 cells. Nonmuscle myosin II concentrations in DFMO-treated cells were decreased by 75%, and stress fibers were sparse or absent. The most striking feature of DFMO-treated cells was the appearance of many small punctate foci of myosin II in the cell interior. Migration of DFMO-treated cells was reduced by 80%. In the presence of DFMO, exogenous putrescine not only returned nonmuscle myosin II levels and distribution toward normal but also restored cell migration to control levels. The administration of wortmannin, an inhibitor of myosin light chain kinase, significantly inhibited cell migration over the denuded area in control cells and in those treated with DFMO + polyamines. These results indicate that 1) polyamine depletion by DFMO is associated with decreased concentration and reorganization of nonmuscle myosin II in IEC-6 cells and 2) exogenous spermidine reverses the inhibitory effects of DFMO.

Differentiated intestinal epithelial cells exhibit increased migration through polyamines and myosin II

1999 ◽  
Vol 277 (6) ◽  
pp. G1149-G1158 ◽  
Author(s):  
Jaladanki N. Rao ◽  
Ji Li ◽  
Li Li ◽  
Barbara L. Bass ◽  
Jian-Ying Wang
Keyword(s):  
Cell Migration ◽  
Epithelial Cells ◽  
Intestinal Epithelial Cells ◽  
Myosin Ii ◽  
Specific Inhibitor ◽  
Intestinal Epithelial ◽  
Nonmuscle Myosin ◽  
Intestinal Crypt ◽  
Nonmuscle Myosin Ii ◽  
Crypt Cells

Early mucosal restitution is a rapid process by which differentiated intestinal epithelial cells migrate to reseal superficial wounds. However, most of the in vitro studies for restitution employ undifferentiated intestinal crypt cells as a model. The transcription factor, Cdx2, plays an important role in the regulation of intestinal epithelial differentiation. Forced expression of the Cdx2 gene in undifferentiated intestinal crypt cells induces the development of a differentiated phenotype. The current study was designed to determine changes in differentiated intestinal epithelial cell migration after wounding in the stable Cdx2-transfected IEC-6 cells and then to examine involvement of polyamines and nonmuscle myosin II in the process of cell motility. Cdx2-transfected IEC-6 cells were associated with a highly differentiated phenotype and exhibited increased cell migration after wounding. Migration of Cdx2-transfected IEC-6 cells were approximately four times that of nontransfected IEC-6 cells. Migration after wounding was associated with significant increases in polyamine synthesis. Depletion of cellular polyamines by 5 mM α-difluoromethylornithine (DFMO), a specific inhibitor of polyamine biosynthesis, inhibited cell migration without affecting the differentiated phenotype. DFMO also decreased levels of nonmuscle myosin II mRNA and protein and resulted in reorganization of myosin II, along with a marked reduction in stress fibers. Exogenous spermidine given together with DFMO not only returned nonmuscle myosin II levels and cellular distribution toward normal but also restored cell migration to control levels. These results indicate that 1) Cdx2-transfected IEC-6 cells exhibit increased cell migration after wounding and 2) cellular polyamines are absolutely required for stimulation of cell migration in association with their ability to modulate the structural organization of nonmuscle myosin II.

scholarly journals Septins are essential for protrusion and detachment in collective border cell migration

2021 ◽  
Author(s):  
Allison M Gabbert ◽  
James Mondo ◽  
Joseph P Campanale ◽  
Denise J Montell
Keyword(s):  
Cell Migration ◽  
Cell Model ◽  
Myosin Ii ◽  
Follicle Cells ◽  
Collective Cell Migration ◽  
Border Cells ◽  
Nonmuscle Myosin ◽  
Border Cell ◽  
Nonmuscle Myosin Ii

Collective cell migration is prevalent throughout development and common in metastatic tumors, yet this process is not fully understood. In this study, we explore the role of septins (Sep) in collective cell migration, using the Drosophila border cell model. We show that Sep2 and Pnut are expressed in migrating border cells and Sep1, 2, 4, and Peanut (Pnut) are required for migration. Pnut stability depends on the expression of Sep1 and Sep2 in epithelial follicle cells and migratory border cells. We show that knockdown of septins prevents normal protrusion and detachment behaviors. High resolution Airyscan imaging reveals Pnut localization in rings at the base of protrusions. While septins function independently of Cdc42, they colocalize dynamically with nonmuscle myosin II. We suggest that septin polymers may stabilize growing protrusions until sufficient myosin is recruited to retract them.

Sign in / Sign up

Export Citation Format

Share Document