LIMD2 is a small lim-only protein overexpressed in metastatic lesions that regulates cell motility and tumor progression by directly binding to and activating the integrin-linked kinase

Cancer Research

Volumn 74, Issue 5, 2014, Pages 1390-1403

  Peng, Hongzhuang ^a   Talebzadeh Farrooji, Mehdi ^f   Osborne, Michael J ^f   Prokop, Jeremy W ^d   McDonald, Paul C ^g   Karar, Jayashree ^a   Hou, Zhaoyuan ^a   He, Mei ^c   Kebebew, Electron ^c   Orntoft, Torben ^e   Herlyn, Meenhard ^a   Caton, Andrew J ^a   Fredericks, William ^b   Malkowicz, Bruce ^b   Paterno, Christopher S ^a   Carolin, Alexandra S ^a   Speicher, David W ^a   Skordalakes, Emmanuel ^a   Huang, Qihong ^a   Dedhar, Shoukat ^g   Borden, Katherine L B ^f   Rauscher, Frank J ^a   more..

^a WISTAR INSTITUTE   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c NATIONAL CANCER INSTITUTE   (United States)

^d UNIVERSITY OF AKRON   (United States)

^e AARHUS UNIVERSITY HOSPITAL   (Denmark)

^f INSTITUTE FOR RESEARCH IN IMMUNOLOGY AND CANCER   (Canada)

^g BRITISH COLUMBIA CANCER RESEARCH CENTRE   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CELL ENZYME; CELL PROTEIN; INTEGRIN LIKED KINASE; LIM PROTEIN; LIM1 PROTEIN; LIMD2 PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING SITE; BLADDER CANCER; BREAST CANCER; CANCER GRADING; CANCER GROWTH; CELL INVASION; CELL LEVEL; CELL MOTILITY; COMPLEX FORMATION; CONTROLLED STUDY; DISEASE ACTIVITY; ENZYME ACTIVITY; ENZYME ASSAY; HUMAN; HUMAN CELL; MELANOMA; METASTASIS; METASTASIS POTENTIAL; MOLECULAR DYNAMICS; MOLECULAR PATHOLOGY; NUCLEAR MAGNETIC RESONANCE IMAGING; PHENOTYPE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; THYROID TUMOR;

ANIMALS; CELL MOVEMENT; DISEASE PROGRESSION; FIBROBLASTS; HEK293 CELLS; HUMANS; LIM DOMAIN PROTEINS; MCF-7 CELLS; MICE; NEOPLASM METASTASIS; NEOPLASMS; PROTEIN BINDING; PROTEIN-SERINE-THREONINE KINASES; SIGNAL TRANSDUCTION;

EID: 84896507744     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-13-1275     Document Type: Article

References (40)

1. Fidler IJ. The pathogenesis of cancer metastasis: the 'seed and soil' hypothesis revisited. Nat Rev Cancer 2003;3:453-8.
2. Sethi N, Kang Y. Unravelling the complexity of metastasis-molecular understanding and targeted therapies. Nat Rev Cancer 2011;11: 735-48.
3. Scott J, Kuhn P, Anderson AR. Unifying metastasis-integrating intravasation, circulation and end-organ colonization. Nat Rev Cancer 2012;12:445-6.
4. Hunter K. Host genetics influence tumour metastasis. Nat Rev Cancer 2006;6:141-6.
5. Alderton GK. Metastasis: epithelial to mesenchymal and back again. Nat Rev Cancer 2013;13:3.
6. Gumireddy K, Huang Q. Identification of metastasis genes by a functional genomics approach. Cell Cycle 2010;9:423.
7. GumireddyK, Li A, GimottyPA, Klein-SzantoAJ, Showe LC, Katsaros D, et al. KLF17 is a negative regulator of epithelial-mesenchymal transition and metastasis in breast cancer. Nat Cell Biol 2009;11:1297-304.
8. Nguyen DX, Bos PD, Massague J. Metastasis: from dissemination to organ-specific colonization. Nat Rev Cancer 2009;9:274-84.
9. Cerutti JM, Oler G, Michaluart P Jr, Delcelo R, Beaty RM, Shoemaker J, et al. Molecular profiling of matched samples identifies biomarkers of papillary thyroid carcinoma lymph node metastasis. Cancer Res 2007; 67:7885-92.
10. Matthews JM, Lester K, Joseph S, Curtis DJ. LIM-domain-only proteins in cancer. Nat Rev Cancer 2013;13:111-22.
11. Chiswell BP, Zhang R, Murphy JW, Boggon TJ, Calderwood DA. The structural basis of integrin-linked kinase-PINCH interactions. Proc Natl Acad Sci U S A 2008;105:20677-82.
12. Peng H, Begg GE, Harper SL, Friedman JR, Speicher DW, Rauscher FJ 3rd. Biochemical analysis of the Kruppel-Associated box (KRAB) transcriptional repression domain. J Biol Chem 2000;275:18000-10.
13. Peng H, Ivanov AV, Oh HJ, Lau YF, Rauscher FJ 3rd. Epigenetic gene silencing by the SRY protein is mediated by a KRAB-O protein that recruits the KAP1 co-repressor machinery. J Biol Chem 2009;284: 35670-80.
14. Pelton JG, Torchia DA, Meadow ND, Roseman S. Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-Transducing protein from Escherichia coli, using twodimensional heteronuclearNMRtechniques. ProteinSci 1993;2:543-58.
15. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A.NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 1995;6:277-93.
16. Goddard TD, Kneller DG (2003), SPARKY (University of California, San Francisco, CA).
17. Morris GM, Huey R, Lindstrom W, Sanner MF, Belew RK, Goodsell DS, et al. AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility. J Comput Chem 2009;30:2785-91.
18. Maydan M, McDonald PC, Sanghera J, Yan J, Rallis C, Pinchin S, et al. Integrin-linked kinase is a functional Mn2+-dependent protein kinase that regulates glycogen synthase kinase-3b (GSK-3b) phosphorylation. PLoS ONE 2010;5:e12356.
19. Kadrmas JL, Beckerle MC. The LIM domain: from the cytoskeleton to the nucleus. Nat Rev Mol Cell Biol 2004;5:920-31.
20. Grishin NV. Treble clef finger-A functionally diverse zinc-binding structural motif. Nucleic Acids Res 2001;29:1703-14.
21. Chiswell BP, Stiegler AL, Razinia Z, Nalibotski E, Boggon TJ, Calderwood DA. Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase. J Struct Biol 2010;170:157-63.
22. Velyvis A, Vaynberg J, Yang Y, Vinogradova O, Zhang Y, Wu C, et al. Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling. Nat Struct Biol 2003;10:558-64.
23. Rooney N, Streuli CH. How integrins control mammary epithelial differentiation: a possible role for the ILK-PINCH-Parvin complex. FEBS Lett 2011;585:1663-72.
24. Sakai T, Li S, Docheva D, Grashoff C, Sakai K, Kostka G, et al. Integrinlinked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation. Genes Dev 2003;17:926-40.
25. Hannigan G, Troussard AA, Dedhar S. Integrin-linked kinase: a cancer therapeutic target unique among its ILK. Nat Rev Cancer 2005;5:51-63.
26. Legate KR, Montanez E, Kudlacek O, Fassler R. ILK, PINCH and parvin: the tIPP of integrin signalling. Nat Rev Mol Cell Biol 2006;7:20-31.
27. Wu C. PINCH, N(i)ck and the ILK: network wiring at cell-matrix adhesions. Trends Cell Biol 2005;15:460-6.
28. Hannigan GE, McDonald PC, Walsh MP, Dedhar S. Integrin-linked kinase: not so 'pseudo' after all. Oncogene 2011;30:4375-85.
29. Fukuda K, Gupta S, Chen K, Wu C, Qin J. The pseudoactive site of ILK is essential for its binding to a-Parvin and localization to focal adhesions. Mol Cell 2009;36:819-30.
30. Velyvis A, Yang Y,WuC, Qin J. Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain. J Biol Chem 2001;276:4932-9.
31. Zhang Y, Chen K, Tu Y, Velyvis A, Yang Y, Qin J, et al. Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites. J Cell Sci 2002;115:4777-86.
32. Persad S, Dedhar S. The role of integrin-linked kinase (ILK) in cancer progression. Cancer Metastasis Rev 2003;22:375-84.
33. Kovalevich J, Tracy B, Langford D. PINCH: more than just an adaptor protein in cellular response. J Cell Physiol 2011;226:940-7.
34. Deng W, Lee J, Wang H, Miller J, Reik A, Gregory PD, et al. Controlling long-range genomic interactions at a native locus by targeted tethering of a looping factor. Cell 2012;149:1233-44.
35. Jing H, Vakoc CR, Ying L, Mandat S, Wang H, Zheng X, et al. Exchange of GATA factors mediates transitions in looped chromatin organization at a developmentally regulated gene locus. Mol Cell 2008;29:232-42.
36. Kuo JC, Han X, Hsiao CT, Yates JR 3rd, Waterman CM. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for b-Pix in negative regulation of focal adhesion maturation. Nat Cell Biol 2011;13:383-93.
37. Hervy M, Hoffman L, Beckerle MC. From the membrane to the nucleus and back again: bifunctional focal adhesion proteins. Curr Opin Cell Biol 2006;18:524-32.
38. Chang DF, Belaguli NS, Iyer D, Roberts WB, Wu SP, Dong XR, et al. Cysteine-rich LIM-only proteins CRP1 and CRP2 are potent smooth muscle differentiation cofactors. Dev Cell 2003;4: 107-18.
39. Hou Z, Peng H, White DE, Negorev DG, Maul GG, Feng Y, et al. LIM protein Ajuba functions as a nuclear receptor corepressor and negatively regulates retinoic acid signaling. Proc Natl Acad Sci U S A 2010;107:2938-43.
40. Hou Z, Peng H, White DE, Wang P, Lieberman PM, Halazonetis T, et al. 14-3-3 binding sites in the snail protein are essential for snail-mediated transcriptional repression and epithelial-mesenchymal differentiation. Cancer Res 2010;70:4385-93.