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1H, 15N and 13C chemical shift assignments of the SH2 domain of human tensin2 (TENC1)

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Abstract

Tensin is an important cytoplasmic phosphoprotein localized to integrin-mediated focal adhesion. It links actin cytoskeleton to extracellular matrix through its N-terminal actin-binding domain and C-terminal phosphotyrosine-binding domain. Studies of knockout mice revealed the critical roles of tensin in skeletal muscle regeneration, renal function and regulation of cell migration. The SH2 domain of tensin interacts with various tyrosine-phosphorylated proteins thus functions as a platform for dis/assembly of signaling molecules. It has also been implicated in recruiting a tumor supperssor protein DLC1 (deleted in live cancer 1) to the focal adhesion, which is required for oncogenic inhibition effect of DLC1 in a phosphotyrosine-independent manner. Here, we report complete chemical shift assignments of the SH2 domain of human tensin2 determined by triple resonance experiments. The resonance assignments serve as a basis for our further functional studies and structure determination by NMR spectroscopy. (BMRB deposits with accession number 16472).

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Acknowledgments

The work described in this paper was supported by a grant from Hong Kong Research Grants Council (RGC664109 and TUYF10SC03 to G.Z). We thank Mr. Feng Rui for helping to set up the NMR experiments.

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Authors and Affiliations

  1. Division of Life Science, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China

    Lihong Chen, Changdong Liu, Feng Rui & Guang Zhu

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  1. Lihong Chen
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  2. Changdong Liu
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  3. Feng Rui
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  4. Guang Zhu
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Correspondence to Guang Zhu.

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Chen, L., Liu, C., Rui, F. et al. 1H, 15N and 13C chemical shift assignments of the SH2 domain of human tensin2 (TENC1). Biomol NMR Assign 5, 211–214 (2011). https://doi.org/10.1007/s12104-011-9302-9

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  • DOI: https://doi.org/10.1007/s12104-011-9302-9

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