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    Mapping the minimum domain of the fibronectin binding site on transglutaminase 2 (TG2) and its importance in mediating signaling, adhesion, and migration in TG2-expressing cells

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    Type
    Article
    Authors
    Soluri, Maria Felicia
    Boccafoschi, Francesca
    Cotella, Diego
    Moro, Laura
    Forestieri, Gabriela
    Autiero, Ida
    Cavallo, Luigi cc
    Oliva, Romina
    Griffin, Martin
    Wang, Zhuo
    Santoro, Claudio
    Sblattero, Daniele
    KAUST Department
    Chemical Science Program
    Computational Bioscience Research Center (CBRC)
    Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
    KAUST Catalysis Center (KCC)
    Physical Science and Engineering (PSE) Division
    Date
    2018-10-04
    Permanent link to this record
    http://hdl.handle.net/10754/630578
    
    Metadata
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    Abstract
    The interaction between the enzyme transglutaminase 2 (TG2) and fibronectin (FN) is involved in the cell-matrix interactions that regulate cell signaling, adhesion, and migration and play central roles in pathologic conditions, particularly fibrosis and cancer. A precise definition of the exact interaction domains on both proteins could provide a tool to design novel molecules with potential therapeutic applications. Although specific residues involved in the interaction within TG2 have been analyzed, little is known regarding the TG2 binding site on FN. This site has been mapped to a large internal 45-kDa protein fragment coincident with the gelatin binding domain (GBD). With the goal of defining the minimal FN interacting domain for TG2, we produced several expression constructs encoding different portions or modules of the GBD and tested their binding and functional properties. The results demonstrate that the I8 module is necessary and sufficient for TG2-binding in vitro, but does not have functional effects on TG2-expressing cells. Modules I7 and I9 increase the strength of the binding and are required for cell adhesion. A 15-kDa fragment encompassing modules I7-9 behaves as the whole 45-kDa GBD and mediates signaling, adhesion, spreading, and migration of TG2+ cells. This study provides new insights into the mechanism for TG2 binding to FN.-Soluri, M. F., Boccafoschi, F., Cotella, D., Moro, L., Forestieri, G., Autiero, I., Cavallo, L., Oliva, R., Griffin, M., Wang, Z., Santoro, C., Sblattero, D. Mapping the minimum domain of the fibronectin binding site on transglutaminase 2 (TG2) and its importance in mediating signaling, adhesion, and migration in TG2-expressing cells.
    Citation
    Soluri MF, Boccafoschi F, Cotella D, Moro L, Forestieri G, et al. (2018) Mapping the minimum domain of the fibronectin binding site on transglutaminase 2 (TG2) and its importance in mediating signaling, adhesion, and migration in TG2-expressing cells. The FASEB Journal: fj.201800054RRR. Available: http://dx.doi.org/10.1096/fj.201800054rrr.
    Publisher
    FASEB
    Journal
    The FASEB Journal
    DOI
    10.1096/fj.201800054rrr
    Additional Links
    https://www.fasebj.org/doi/10.1096/fj.201800054RRR
    ae974a485f413a2113503eed53cd6c53
    10.1096/fj.201800054rrr
    Scopus Count
    Collections
    Articles; Physical Science and Engineering (PSE) Division; Chemical Science Program; KAUST Catalysis Center (KCC); Computational Bioscience Research Center (CBRC); Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division

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