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      Coiling and maturation of a high-performance fibre in hagfish slime gland thread cells

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          Abstract

          The defensive slime of hagfishes contains thousands of intermediate filament protein threads that are manufactured within specialized gland thread cells. The material properties of these threads rival those of spider dragline silks, which makes them an ideal model for biomimetic efforts to produce sustainable protein materials, yet how the thread is produced and organized within the cell is not well understood. Here we show how changes in nuclear morphology, size and position can explain the three-dimensional pattern of thread coiling in gland thread cells, and how the ultrastructure of the thread changes as very young thread cells develop into large cells with fully mature coiled threads. Our model provides an explanation for the complex process of thread assembly and organization that has fascinated and perplexed biologists for over a century, and provides valuable insights for the quest to manufacture high-performance biomimetic protein materials.

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          Demonstration of mechanical connections between integrins, cytoskeletal filaments, and nucleoplasm that stabilize nuclear structure

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            Nuclear positioning.

            The nucleus is the largest organelle and is commonly depicted in the center of the cell. Yet during cell division, migration, and differentiation, it frequently moves to an asymmetric position aligned with cell function. We consider the toolbox of proteins that move and anchor the nucleus within the cell and how forces generated by the cytoskeleton are coupled to the nucleus to move it. The significance of proper nuclear positioning is underscored by numerous diseases resulting from genetic alterations in the toolbox proteins. Finally, we discuss how nuclear position may influence cellular organization and signaling pathways. Copyright © 2013 Elsevier Inc. All rights reserved.
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              ‘Hard’ and ‘soft’ principles defining the structure, function and regulation of keratin intermediate filaments

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                Author and article information

                Journal
                Nature Communications
                Nat Commun
                Springer Science and Business Media LLC
                2041-1723
                May 2014
                April 4 2014
                May 2014
                : 5
                : 1
                Article
                10.1038/ncomms4534
                24698953
                e839611b-1788-474b-9855-f88eb1c95a2a
                © 2014

                http://www.springer.com/tdm

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