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Solution structure of the phosphotyrosine binding (PTB) domain of human tensin2 protein in complex with deleted in liver cancer 1 (DLC1) peptide reveals a novel peptide binding mode.

Chen L, Liu C, Ko FC, Xu N, Ng IO, Yam JW, Zhu G.

J Biol Chem. 2012 Jul 27;287(31):26104-14. doi: 10.1074/jbc.M112.360206. Epub 2012 May 29.


Deleted in liver cancer 1 (DLC1) utilizes a novel binding site for Tensin2 PTB domain interaction and is required for tumor-suppressive function.

Chan LK, Ko FC, Ng IO, Yam JW.

PLoS One. 2009;4(5):e5572. doi: 10.1371/journal.pone.0005572. Epub 2009 May 15.


Interaction of deleted in liver cancer 1 with tensin2 in caveolae and implications in tumor suppression.

Yam JW, Ko FC, Chan CY, Jin DY, Ng IO.

Cancer Res. 2006 Sep 1;66(17):8367-72.


START-GAP1/DLC1 is localized in focal adhesions through interaction with the PTB domain of tensin2.

Kawai K, Kitamura SY, Maehira K, Seike J, Yagisawa H.

Adv Enzyme Regul. 2010;50(1):202-15. doi: 10.1016/j.advenzreg.2009.10.013. Epub 2009 Nov 4. No abstract available.


Solution structure of tensin2 SH2 domain and its phosphotyrosine-independent interaction with DLC-1.

Dai K, Liao S, Zhang J, Zhang X, Tu X.

PLoS One. 2011;6(7):e21965. doi: 10.1371/journal.pone.0021965. Epub 2011 Jul 12.


Individual domains of Tensin2 exhibit distinct subcellular localisations and migratory effects.

Hafizi S, Sernstad E, Swinny JD, Gomez MF, Dahlbäck B.

Int J Biochem Cell Biol. 2010 Jan;42(1):52-61. doi: 10.1016/j.biocel.2009.09.005. Epub 2009 Sep 9.


Full activity of the deleted in liver cancer 1 (DLC1) tumor suppressor depends on an LD-like motif that binds talin and focal adhesion kinase (FAK).

Li G, Du X, Vass WC, Papageorge AG, Lowy DR, Qian X.

Proc Natl Acad Sci U S A. 2011 Oct 11;108(41):17129-34. doi: 10.1073/pnas.1112122108. Epub 2011 Oct 3.


Oncogenic inhibition by a deleted in liver cancer gene requires cooperation between tensin binding and Rho-specific GTPase-activating protein activities.

Qian X, Li G, Asmussen HK, Asnaghi L, Vass WC, Braverman R, Yamada KM, Popescu NC, Papageorge AG, Lowy DR.

Proc Natl Acad Sci U S A. 2007 May 22;104(21):9012-7. Epub 2007 May 15.


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

Chen L, Liu C, Rui F, Zhu G.

Biomol NMR Assign. 2011 Oct;5(2):211-4. doi: 10.1007/s12104-011-9302-9. Epub 2011 Apr 3.


The protein-tyrosine kinase Syk interacts with the C-terminal region of tensin2.

Moon KD, Zhang X, Zhou Q, Geahlen RL.

Biochim Biophys Acta. 2012 Feb;1823(2):199-205. doi: 10.1016/j.bbamcr.2011.10.001. Epub 2011 Oct 12.


CDK5 is a major regulator of the tumor suppressor DLC1.

Tripathi BK, Qian X, Mertins P, Wang D, Papageorge AG, Carr SA, Lowy DR.

J Cell Biol. 2014 Dec 8;207(5):627-42. doi: 10.1083/jcb.201405105. Epub 2014 Dec 1.


Differential regulation of the activity of deleted in liver cancer 1 (DLC1) by tensins controls cell migration and transformation.

Cao X, Voss C, Zhao B, Kaneko T, Li SS.

Proc Natl Acad Sci U S A. 2012 Jan 31;109(5):1455-60. doi: 10.1073/pnas.1114368109. Epub 2012 Jan 17. Erratum in: Proc Natl Acad Sci U S A. 2012 Mar 20;109(12):4708.


Interaction of DISC1 with the PTB domain of Tensin2.

Goudarzi S, Smith LJ, Schütz S, Hafizi S.

Cell Mol Life Sci. 2013 May;70(9):1663-72. doi: 10.1007/s00018-012-1228-6. Epub 2012 Dec 12.


Tensin1 and a previously undocumented family member, tensin2, positively regulate cell migration.

Chen H, Duncan IC, Bozorgchami H, Lo SH.

Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):733-8. Epub 2002 Jan 15.


Tensin1 positively regulates RhoA activity through its interaction with DLC1.

Shih YP, Sun P, Wang A, Lo SH.

Biochim Biophys Acta. 2015 Dec;1853(12):3258-65. doi: 10.1016/j.bbamcr.2015.09.028. Epub 2015 Sep 28.


START-GAP2/DLC2 is localized in focal adhesions via its N-terminal region.

Kawai K, Seike J, Iino T, Kiyota M, Iwamae Y, Nishitani H, Yagisawa H.

Biochem Biophys Res Commun. 2009 Mar 20;380(4):736-41. doi: 10.1016/j.bbrc.2009.01.095. Epub 2009 Jan 23.


Structure of the C-terminal phosphotyrosine interaction domain of Fe65L1 complexed with the cytoplasmic tail of amyloid precursor protein reveals a novel peptide binding mode.

Li H, Koshiba S, Hayashi F, Tochio N, Tomizawa T, Kasai T, Yabuki T, Motoda Y, Harada T, Watanabe S, Inoue M, Hayashizaki Y, Tanaka A, Kigawa T, Yokoyama S.

J Biol Chem. 2008 Oct 3;283(40):27165-78. doi: 10.1074/jbc.M803892200. Epub 2008 Jul 23.


Characterization of DLC1-SAM equilibrium unfolding at the amino acid residue level.

Yang S, Noble CG, Yang D.

Biochemistry. 2009 May 19;48(19):4040-9. doi: 10.1021/bi9000936.


LD Motif Recognition by Talin: Structure of the Talin-DLC1 Complex.

Zacharchenko T, Qian X, Goult BT, Jethwa D, Almeida TB, Ballestrem C, Critchley DR, Lowy DR, Barsukov IL.

Structure. 2016 Jul 6;24(7):1130-41. doi: 10.1016/j.str.2016.04.016. Epub 2016 Jun 2.

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