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April 1, 2017
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cess article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Funding: This work was funded by a generous donation from the Litwin foundation and the U.S. Public Health grant CA100687 from the National Cancer Institute, National Institutes of Health, and Department of Health and Human Services. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. Competing Interests: The authors have read the journal’s policy and have the following conflicts: the contents of this paper are being utilized for a patent. According to the rules and regulations of New York University School of Medicine, if this patent is licensed by a third party, the authors may receive benefits in the form of royalties or equity participation. This does not alter their adherence to all the PLoS ONE policies on sharing data and materials. E-mail: [email protected] Introduction associated and involved in maturation of the 40S ribosome, specifically processing of the 20S to 18S rRNA. In addition, LamR plays a role in maintaining cell viability in yeast and in a number of human cells. Previous studies have also implicated 67 kDa LamR in binding interactions with actin at the cell membrane. A 70 kDa cell-surface protein, originally called connectin, was found to bind both laminin and actin in vitro. It was also found that clustering of laminin in the ECM results in LamR clustering and subsequent actin remodeling. Further, a 69 kDa Gypenoside IX laminin-binding protein was found to interact with microfilaments to mediate cell attachment and migration. These data indicate that LamR interactions with the cytoskeleton might play a role in cell motility. The cytoskeleton, an elaborate network of proteins, is responsible for providing structure and shape to the cell and manipulating the cell membrane to induce cell motility. This network is comprised of three main types of proteins: microfilaments comprised of helical assemblies of actin, microtubules comprised of alpha and beta tubulin dimers and intermediate filaments comprised of a number of different proteins, depending on cell type. The cytoskeleton is also associated with many cellular components such as the nucleus, the cell membrane, vesicles and other macromolecules. This protein meshwork acts as a highway connecting different points of the cell and utilizing molecular motors powered by filament assembly forces to transport proteins and organelles across the cell’s span. In response to migration-inducing stimuli, actin January 2011 | Volume 6 | Issue 1 | e15895 Laminin Receptor and the Cytoskeleton repolymerizes, polarizing the cell and enabling the formation of lamellipodia and filapodia protrusions. These protrusions, which are stabilized by transmembrane receptors interacting with the ECM, enable the cell to crawl by the use of these adhesions at the leading edge. In addition, the cytoskeleton plays a role in cellular translation. It was originally thought that translation of select transcripts occurred at the cytoskeleton, however new evidence indicates that a significant portion of translation may occur bound 9373158 to the cytoskeleton. Immunofluorescence staining and electron microscopy indicates that polysomes colocalize with cytoskeletal components. Detergent treatment of cells, which removes polysomes bound to the en