Zyxin and paxillin proteins: focal adhesion plaque LIM domain proteins go nuclear.

Zyxin and paxillin are the prototypes of two related subfamilies of LIM domain proteins that are localized primarily at focal adhesion plaques. However, recent work has shown that zyxin/paxillin family proteins also shuttle through the nucleus. These proteins may enter the nucleus by association with other proteins, but are exported from the nucleus by means of intrinsic leucine-rich nuclear export sequences. Zyxin/paxillin proteins may regulate gene transcription by interaction with transcription factors. In some cases, misregulation of nuclear functions of zyxin/paxillin proteins appear to be associated with pathogenic effects.

[1]  T. Rabbitts,et al.  Perspective: chromosomal translocations can affect genes controlling gene expression and differentiation—why are these functions targeted? , 1999, The Journal of pathology.

[2]  P. Rogalla,et al.  An identical HMGIC‐LPP fusion transcript is consistently expressed in pulmonary chondroid hamartomas with t(3;12)(q27–28;q14–15) , 2000, Genes, chromosomes & cancer.

[3]  T. Gilmore,et al.  LIM domain protein Trip6 has a conserved nuclear export signal, nuclear targeting sequences, and multiple transactivation domains. , 2001, Biochimica et biophysica acta.

[4]  M. Roberts,et al.  Paxillin Associates with Poly(A)-binding Protein 1 at the Dense Endoplasmic Reticulum and the Leading Edge of Migrating Cells* , 2002, The Journal of Biological Chemistry.

[5]  D. DeFranco,et al.  Interaction of the tau2 transcriptional activation domain of glucocorticoid receptor with a novel steroid receptor coactivator, Hic-5, which localizes to both focal adhesions and the nuclear matrix. , 2000, Molecular biology of the cell.

[6]  U. Gaul,et al.  A novel muscle LIM‐only protein is generated from the paxillin gene locus in Drosophila , 2001, EMBO reports.

[7]  K. Mimori,et al.  Characterization of the human TESTIN gene localized in the FRA7G region at 7q31.2. , 2000, Genomics.

[8]  K. Kamiguchi,et al.  Interaction of Hic-5, A Senescence-related Protein, with Focal Adhesion Kinase* , 1998, The Journal of Biological Chemistry.

[9]  D. Sun,et al.  Lepidopteran DALP, and its mammalian ortholog HIC-5, function as negative regulators of muscle differentiation. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[10]  M. Sheng,et al.  Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2 , 2000, Nature.

[11]  C. Missero,et al.  The DNA Glycosylase T:G Mismatch-specific Thymine DNA Glycosylase Represses Thyroid Transcription Factor-1-activated Transcription* , 2001, The Journal of Biological Chemistry.

[12]  W. V. D. Van de Ven,et al.  LPP, the preferred fusion partner gene of HMGIC in lipomas, is a novel member of the LIM protein gene family. , 1996, Genomics.

[13]  M. Beckerle,et al.  LIM domain-containing protein trip6 can act as a coactivator for the v-Rel transcription factor. , 1999, Gene expression.

[14]  Hiroaki Honda,et al.  Members of the Zyxin Family of LIM Proteins Interact with Members of the p130Cas Family of Signal Transducers* , 2002, The Journal of Biological Chemistry.

[15]  C. Turner,et al.  Association of Bovine Papillomavirus Type 1 E6 oncoprotein with the focal adhesion protein paxillin through a conserved protein interaction motif , 1998, Oncogene.

[16]  R. Brent,et al.  Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. , 1995, Molecular endocrinology.

[17]  S. Inui,et al.  Cloning and Characterization of Androgen Receptor Coactivator, ARA55, in Human Prostate* , 1999, The Journal of Biological Chemistry.

[18]  Michael D Schaller,et al.  Paxillin: a focal adhesion-associated adaptor protein , 2001, Oncogene.

[19]  M. Ishino,et al.  Nuclear Translocation of Cell Adhesion Kinase β/Proline-rich Tyrosine Kinase 2 , 2002 .

[20]  David A. Nix,et al.  Nuclear–Cytoplasmic Shuttling of the Focal Contact Protein, Zyxin: A Potential Mechanism for Communication between Sites of Cell Adhesion and the Nucleus , 1997, The Journal of cell biology.

[21]  S. Bockholt,et al.  Targeting of Zyxin to Sites of Actin Membrane Interaction and to the Nucleus* , 2001, The Journal of Biological Chemistry.

[22]  Kenneth M. Yamada,et al.  Transmembrane crosstalk between the extracellular matrix and the cytoskeleton , 2001, Nature Reviews Molecular Cell Biology.

[23]  A Brizard,et al.  Human LPP gene is fused to MLL in a secondary acute leukemia with a t(3;11) (q28;q23) , 2001, Genes, chromosomes & cancer.

[24]  N. Perrimon,et al.  The Promise and Perils of Wnt Signaling Through β-Catenin , 2002, Science.

[25]  S. Silverstein,et al.  Interaction of Zyxin, a Focal Adhesion Protein, with the E6 Protein from Human Papillomavirus Type 6 Results in Its Nuclear Translocation , 2001, Journal of Virology.

[26]  H. Marie,et al.  Ajuba, a cytosolic LIM protein, shuttles into the nucleus and affects embryonal cell proliferation and fate decisions. , 2000, Molecular biology of the cell.

[27]  K. Nose,et al.  The LIM domains of hic-5 protein recognize specific DNA fragments in a zinc-dependent manner in vitro. , 1998, Nucleic acids research.

[28]  R. Pardi,et al.  Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity , 2000, Nature.

[29]  Sheila M. Thomas,et al.  Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin. , 1999, Journal of cell science.

[30]  P. Howley,et al.  The bovine papillomavirus E6 oncoprotein interacts with paxillin and disrupts the actin cytoskeleton. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[31]  M. Beckerle.  Zyxin: Zinc fingers at sites of cell adhesion , 1997, BioEssays : news and reviews in molecular, cellular and developmental biology.

[32]  W. V. D. Van de Ven,et al.  LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity. , 2000, Molecular biology of the cell.

[33]  T. Gilmore,et al.  Characterization of mouse Trip6: a putative intracellular signaling protein. , 1999, Gene.

[34]  P. Rogalla,et al.  A novel LPP fusion gene indicates the crucial role of truncated LPP proteins in lipomas and pulmonary chondroid hamartomas , 2002, Cytogenetic and Genome Research.

[35]  J. Fletcher,et al.  Disruption of the architectural factor HMGI-C: DNA-binding AT hook motifs fused in lipomas to distinct transcriptional regulatory domains , 1995, Cell.