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      Visualization of Src and FAK Activity during the Differentiation Process from HMSCs to Osteoblasts

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          Abstract

          Non-receptor protein kinases FAK and Src play crucial roles in regulating cellular adhesions, growth, migration and differentiation. However, it remains unclear how the activity of FAK and Src is regulated during the differentiation process from mesenchymal stem cells (MSCs) to bone cells. In this study, we used genetically encoded FAK and Src biosensors based on fluorescence resonance energy transfer (FRET) to monitor the FAK and Src activity in live cells during the differentiation process. The results revealed that the FAK activity increased after the induction of differentiation, which peaked around 20–27 days after induction. Meanwhile, the Src activity decreased continuously for 27 days after induction. Therefore, the results showed significant and differential changes of FAK and Src activity upon induction. This opposite trend between FAK and Src activation suggests novel and un-coupled Src/FAK functions during the osteoblastic differentiation process. These results should provide important information for the biochemical signals during the differentiation process of stem cells toward bone cells, which will advance our understanding of bone repair and tissue engineering.

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          The green fluorescent protein.

          R Tsien (1998)
          In just three years, the green fluorescent protein (GFP) from the jellyfish Aequorea victoria has vaulted from obscurity to become one of the most widely studied and exploited proteins in biochemistry and cell biology. Its amazing ability to generate a highly visible, efficiently emitting internal fluorophore is both intrinsically fascinating and tremendously valuable. High-resolution crystal structures of GFP offer unprecedented opportunities to understand and manipulate the relation between protein structure and spectroscopic function. GFP has become well established as a marker of gene expression and protein targeting in intact cells and organisms. Mutagenesis and engineering of GFP into chimeric proteins are opening new vistas in physiological indicators, biosensors, and photochemical memories.
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            Integrin-regulated FAK-Src signaling in normal and cancer cells.

            Satyajit K. Mitra, David Schlaepfer (2006)
            Integrins can alter cellular behavior through the recruitment and activation of signaling proteins such as non-receptor tyrosine kinases including focal adhesion kinase (FAK) and c-Src that form a dual kinase complex. The FAK-Src complex binds to and can phosphorylate various adaptor proteins such as p130Cas and paxillin. In normal cells, multiple integrin-regulated linkages exist to activate FAK or Src. Activated FAK-Src functions to promote cell motility, cell cycle progression and cell survival. Recent studies have found that the FAK-Src complex is activated in many tumor cells and generates signals leading to tumor growth and metastasis. As both FAK and Src catalytic activities are important in promoting VEGF-associated tumor angiogenesis and protease-associated tumor metastasis, support is growing that FAK and Src may be therapeutically relevant targets in the inhibition of tumor progression.
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              FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly.

              Donna J Webb, Karen Donais, Leanna Whitmore … (2004)
              Cell migration is a complex, highly regulated process that involves the continuous formation and disassembly of adhesions (adhesion turnover). Adhesion formation takes place at the leading edge of protrusions, whereas disassembly occurs both at the cell rear and at the base of protrusions. Despite the importance of these processes in migration, the mechanisms that regulate adhesion formation and disassembly remain largely unknown. Here we develop quantitative assays to measure the rate of incorporation of molecules into adhesions and the departure of these proteins from adhesions. Using these assays, we show that kinases and adaptor molecules, including focal adhesion kinase (FAK), Src, p130CAS, paxillin, extracellular signal-regulated kinase (ERK) and myosin light-chain kinase (MLCK) are critical for adhesion turnover at the cell front, a process central to migration.
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                Author and article information

                Contributors
                : Role: Editor
                Journal
                Journal ID (nlm-ta): PLoS One
                Journal ID (iso-abbrev): PLoS ONE
                Journal ID (publisher-id): plos
                Journal ID (pmc): plosone
                Title: PLoS ONE
                Publisher: Public Library of Science (San Francisco, USA )
                ISSN (Electronic): 1932-6203
                Publication date Collection: 2012
                Publication date (Electronic): 10 August 2012
                Volume: 7
                Issue: 8
                Electronic Location Identifier: e42709
                Affiliations
                [1 ]Biomaterials and Live Cell Imaging Institute, School of Metallurgy and Materials Engineering, Chongqing University of Science and technology, Chongqing, People’s Republic of China
                [2 ]Department of Bioengineering, University of Illinois, Urbana-Champaign, Urbana, Illinois, United States of America
                [3 ]Beckman Institute for Advanced Science and Technology, Center for Biophysics and Computational Biology, Institute for Genomic Biology, Department of Integrative and Molecular Physiology, University of Illinois, Urbana-Champaign, Urbana, Illinois, United States of America
                National Centre for Scientific Research, ‘Demokritos’, Greece
                Author notes

                Competing Interests: The authors have declared that no competing interests exist.

                Conceived and designed the experiments: XL SL YW. Performed the experiments: XL. Analyzed the data: XL SL YZ CW WX YW. Contributed reagents/materials/analysis tools: YW. Wrote the paper: XL SL YZ CW WX YW.

                Article
                Publisher ID: PONE-D-12-06619
                DOI: 10.1371/journal.pone.0042709
                PMC ID: 3416797
                PubMed ID: 22900044
                SO-VID: c1eb4923-6440-4eb9-b2d9-df610ec1b23c
                Copyright statement: Copyright @ 2012
                License:

                This is an open-access 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.

                History
                Date received : 4 March 2012
                Date accepted : 11 July 2012
                Page count
                Pages: 7
                Funding
                This work was supported in part by grants from NIH HL098472, NS063405, NSF CBET0846429 (Y.W., S.L. and C.W.), Research Foundation of University of Illinois (S.L.) and the Natural Science Key Foundation Project of CQ in China (CSTC2012JJB0097), and Research Foundation of Chongqing University of Science & Technology (CK2010B18, CK2011Z03) (X.L., W.X.). Y.Z. was supported by the Beckman Graduate Fellowship.
                Categories
                Subject: Research Article
                Subject: Biology
                Subject: Anatomy and Physiology
                Subject: Musculoskeletal System
                Subject: Bone
                Subject: Biotechnology
                Subject: Tissue Engineering
                Subject: Developmental Biology
                Subject: Stem Cells
                Subject: Mesenchymal Stem Cells
                Subject: Cell Differentiation
                Subject: Molecular Cell Biology
                Subject: Signal Transduction
                Subject: Signaling Cascades
                Subject: Protein Kinase Signaling Cascade

                ScienceOpen disciplines: Uncategorized
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