Cell matrix adhesions in cancer: The proteins that form the glue

Mazvita Maziveyi and Suresh K. Alahari _

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Oncotarget. 2017; 8:48471-48487. https://doi.org/10.18632/oncotarget.17265

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Mazvita Maziveyi1 and Suresh K. Alahari1

1Department of Biochemistry and Molecular Biology, Stanley S. Scott Cancer Center, Louisiana State University Health Sciences Center, New Orleans, LA, USA

Correspondence to:

Suresh K. Alahari, email: salaha@lsuhsc.edu

Keywords: integrins, cancer, focal adhesions

Received: November 16, 2016     Accepted: March 27, 2017     Published: April 20, 2017


The main purposes of Integrin-mediated cell contacts are to interpret bi-directional signals between the extracellular environment and intracellular proteins, as well as, anchor the cell to a matrix. Many cell adhesion molecules have been discovered with a wide spectrum of responsibilities, including recruiting, activating, elongating, and maintaining. This review will perlustrate some of the key incidences that precede focal adhesion formation. Tyrosine phosphorylation is a key signaling initiation event that leads to the recruitment of multiple proteins to focal adhesion sites. Recruitment and concentration of proteins such as Paxillin and Vinculin to Integrin clutches is necessary for focal adhesion development. The assembled networks are responsible for transmitting signals back and forth from the extracellular matrix (ECM) to Actin and its binding proteins. Cancer cells exhibit highly altered focal adhesion dynamics. This review will highlight some key discoveries in cancer cell adhesion, as well as, identify current gaps in knowledge.

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