Myosin light-chain kinase contributes to the proliferation and migration of breast cancer cells through cross-talk with activated ERK1/2.

Zhou X; Liu Y; You J; Zhang H; Zhang X; Ye L

doi:10.1016/j.canlet.2008.05.028

Myosin light-chain kinase contributes to the proliferation and migration of breast cancer cells through cross-talk with activated ERK1/2.

Zhou X ¹,

Liu Y ,

You J ,

Zhang H ,

Zhang X ,

Ye L

Affiliations

1. Department of Biochemistry, College of Life Sciences, Nankai University, Tianjin 300071, PR China.
Authors
Zhou X¹
(1 author)

Cancer Letters, 16 Aug 2008, 270(2):312-327
https://doi.org/10.1016/j.canlet.2008.05.028 PMID: 18710790

Abstract

Myosin light-chain kinase (MLCK) plays a crucial role in the cell migration and tumor metastasis. Herein, we investigated the signaling pathways involved in MLCK using ML-7, a specific inhibitor of MLCK, in breast cancer cell proliferation and migration. Our data showed that reduction of MLCK in breast cancer cells mediated by 20 microM ML-7 was able to depress the cell proliferation and migration using two parallel cell lines (MCF-7 and LM-MCF/MDA-MB-231) with different metastatic abilities through reciprocal cross-talk with activated ERK1/2, in which both phosphorylated myosin light chain (p-MLC) and cascades of beta-catenin, cyclin D1, survivin, and c-Myc serve as essential downstream effectors.

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Read article at publisher's site: https://doi.org/10.1016/j.canlet.2008.05.028

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Proteins in UniProt (Showing 5 of 11)

mitogen-activated protein kinase(UniProt - A1QJE5)
Mitogen-activated protein kinase(UniProt - B4DHN0)
mitogen-activated protein kinase(UniProt - Q8NHX0)
Mitogen-activated protein kinase(UniProt - L7RXH5)
Mitogen-activated protein kinase 3(UniProt - P27361)

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GlyGen is an international glycobioinformatics knowledgebase funded by The National Institutes of Health to facilitate glycoscience research by integrating diverse kinds of information, including glycomics, genomics, proteomics (and glycoproteomics), cell biology, developmental biology and biochemistry.

https://www.glygen.org/publication/MED/18710790

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Myosin light-chain kinase contributes to the proliferation and migration of breast cancer cells through cross-talk with activated ERK1/2.

Affiliations

Authors

Abstract

Full text links

References

Breast cancer metastasis: markers and models.

A specific isoform of nonmuscle myosin II-C is required for cytokinesis in a tumor cell line.

Myosin IIA regulates cell motility and actomyosin-microtubule crosstalk.

Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells.

A fluorescent resonant energy transfer-based biosensor reveals transient and regional myosin light chain kinase activation in lamella and cleavage furrows.

Asymmetric distribution of myosin IIB in migrating endothelial cells is regulated by a rho-dependent kinase and contributes to tail retraction.

Use of DNA sequence and mutant analyses and antisense oligodeoxynucleotides to examine the molecular basis of nonmuscle myosin light chain kinase autoinhibition, calmodulin recognition, and activity.

Stable transfectants of smooth muscle cell line lacking the expression of myosin light chain kinase and their characterization with respect to the actomyosin system.

Na+–K+–2Cl− cotransport in Ehrlich cells: regulation by protein phosphatases and kinases

An increase or a decrease in myosin II phosphorylation inhibits macrophage motility.

Citations & impact

Impact metrics

Citations of article over time

Article citations

Loss of myosin light chain kinase induces the cellular senescence associated secretory phenotype to promote breast epithelial cell migration.

METTL5 serves as a diagnostic and prognostic biomarker in hepatocellular carcinoma by influencing the immune microenvironment.

Core fucosylation and its roles in gastrointestinal glycoimmunology.

Elevation of Cytoplasmic Calcium Suppresses Microtentacle Formation and Function in Breast Tumor Cells.

A Drug Screening Reveals Minocycline Hydrochloride as a Therapeutic Option to Prevent Breast Cancer Cells Extravasation across the Blood-Brain Barrier.

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Myosin light-chain kinase contributes to the proliferation and migration of breast cancer cells through cross-talk with activated ERK1/2.

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Abstract

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Na+–K+–2Cl− cotransport in Ehrlich cells: regulation by protein phosphatases and kinases

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