ArticleAmerican journal of physiology. Cell physiology2011
The phosphorylation state of MRLC is polyamine dependent in intestinal epithelial cells.
Article in American journal of physiology. Cell physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- A genetic model of congenital intestinal atresia implicates Mypt1 in epithelial organisation.Disease models & mechanisms · 2026Article
- MRLC controls apoptotic cell death and functions to regulate epidermal development during planarian regeneration and homeostasis.Cell proliferation · 2024Article
- Scribble, Lgl1, and myosin IIA interact with α-/β-catenin to maintain epithelial junction integrity.Cell adhesion & migration · 2023Article
- Spermine protects intestinal barrier integrity through ras-related C3 botulinum toxin substrate 1/phospholipase C-γ1 signaling pathway in piglets.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2022Article
- Absence of keratins 8 and 18 in rodent epithelial cell lines associates with keratin gene mutation and DNA methylation: Cell line selective effects on cell invasion.Experimental cell research · 2015Article
- Defining suitable reference genes for RT-qPCR analysis on intestinal epithelial cells.Molecular biotechnology · 2013Article
- Polyamines and Gut Mucosal Homeostasis.Journal of gastrointestinal & digestive system · 2012Article
- Activation of Dbl restores migration in polyamine-depleted intestinal epithelial cells via Rho-GTPases.American journal of physiology. Gastrointestinal and liver physiology · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Cell migration is important to the integrity of the gastrointestinal tract for the normal movement of cells from crypt to villi and the healing of wounds. Polyamines are essential to cell migration, mucosal restitution, and, hence, healing. Polyamine depletion by α-difluoromethyl ornithine (DFMO) inhibited migration by decreasing lamellipodia and stress fiber formation and preventing the activation of Rho-GTPases. Polyamine depletion increased the association of the thick F-actin cortex with phosphorylated myosin regulatory light chain (pMRLC). In this study, we determined why MRLC is constitutively phosphorylated as part of the actin cortex. Inhibition of myosin light chain kinase (MLCK) decreased RhoA and Rac1 activities and significantly inhibited migration. Polyamine depletion increased phosphorylation of MRLC (Thr18/Ser19) and stabilized the actin cortex and focal adhesions. The Rho-kinase inhibitor Y27632 increased spreading and migration by decreasing the phosphorylation of MRLC, remodeling focal adhesions, and by activating Rho-GTPases. Thus phosphorylation of MRLC appears to be the rate-limiting step during the migration of IEC-6 cells. In addition, increased localization of RhoA with the actin cortex in polyamine-depleted cells appears to activate Rho-kinase. In the absence of polyamines, activated Rho-kinase phosphorylates myosin phosphatase targeting subunit 1 (MYPT1) at serine-668 leading to its inactivation and preventing the recruitment of phosphatase (protein phosphastase, PP1cδ) to the actomyosin cortex. In this condition, MRLC is constitutively phosphorylated and cycling does not occur. Thus activated myosin binds F-actin stress fibers and prevents focal adhesion turnover, Rho-GTPase activation, and the remodeling of the cytoskeleton required for migration.
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