Parallel Association of Fos and Jun Leucine Zippers Juxtaposes DNA Binding Domains

Gentz, Reiner; Rauscher, Frank J.; Abate, Cory; Curran, Tom

doi:10.1126/science.2494702

Cited by 568 publications

(324 citation statements)

References 30 publications

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“…Moreover, the conformational analysis of CT-8/ HOM-TES-85 with di erent algorithms strongly suggested the presence of an N-terminal helical structure. In fact, in DNA-binding leucine zipper molecules the zipper region is regularly located in the C-terminus and is responsible for mediating speci®c protein dimerization (Kouzarides and Zi , 1988;Gentz et al, 1989;Turner and Tjian, 1989), which in turn is an essential prerequisite for DNA-binding activity of an N-terminal basic region. The sequence analysis being suggestive for involvement of CT-8/ HOM-TES-85 in transcriptional processes, we wanted to focus our studies on the subcellular localization of this protein, which may also be indicative of functional properties of this molecule.…”

Section: Discussionmentioning

confidence: 99%

A novel tumour associated leucine zipper protein targeting to sites of gene transcription and splicing

et al. 2002

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We describe here the de®nition and characterization of antigen CT-8/HOM-TES-85 encoded by a previously unknown gene and identi®ed by serological expression screening using antibodies from a seminoma patient. Intriguingly, the leucine zipper region of CT-8/HOM-TES-85 shows an atypical amphipathy with clusters of hydrophobic residues that is exclusively shared by the Nmyc proto-oncogene. CT-8/HOM-TES-85 gene is tightly silenced in normal tissues except for testis. However, it is frequently activated in human neoplasms of di erent types including lung cancer, ovarian cancer, melanoma and glioma. Endogenous as well as heterogeneously expressed CT-8/HOM-TES-85 targets predominantly to the nucleus forming a distinctive speckled pattern of nuclear dots arranged in macromolecular structures. By co-localization studies these speckles were identi®ed as loci of transcriptional activity and splicing, suggesting that CT-8/HOM-TES-85 may be involved in these processes. The aberrant expression of CT-8/HOM-TES-85 in human neoplasms might therefore be involved in cancer associated alterations of transcriptional or post-transcriptional processes and thus may disclose new mechanisms involved in the manifestation of the cancer phenotype.

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Section: Discussionmentioning

confidence: 99%

A novel tumour associated leucine zipper protein targeting to sites of gene transcription and splicing

et al. 2002

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“…This phenotype suggests that the expression of a truncated SIP3 protein, containing only the first 409 amino acids, is detrimental during growth on glucose. The amount of invertase produced in the sip3A1::HIS3 strain under derepressing conditions was 2.5 times lower than in the wild type ( (32) and to mediate dimer formation (33,34,35 (5). Third, the overexpression of the GBDSIP311o7 hybrid protein caused slow growth of strain GGY::171 on glucose and also impaired the derepression of SUC2 in the wild-type strain MCY829.…”

Section: Disruption Of the Sip3 Chromosomal Locusmentioning

confidence: 99%

Analysis of the SIP3 protein identified in a two-hybrid screen for interaction with the SNF1 protein kinase

1994

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The Saccharomyces cerevisiae SIP3 gene was identified in a two-hybrid screen for proteins that interact in vivo with the SNF1 protein kinase, which is necessary for release of glucose repression. We showed that the C-terminal part of SIP3, recovered through its ability to interact with SNF1, strongly activates transcription when tethered to DNA. We have cloned and sequenced the entire SIP3 gene. The predicted 142-kD SIP3 protein contains a putative leucine zipper motif located in its C terminus. The native SIP3 protein also interacts with DNA-bound SNF1 and activates transcription of a target gene. A complete deletion of the SIP3 gene did not confer phenotypes characteristic of snfl mutants. However, in a mutant deficient for the SNF1 kinase activity due to loss of the SNF4 stimulatory function, increased dosage of SIP3 partially restored expression of the glucose-repressible SUC2 gene. Overexpression of the C terminus of SIP3 caused defects in growth and SUC2 expression which were remedied by overexpressing SNF1. Taken together, these genetic data suggest that SIP3 is functionally related to the SNF1 protein kinase pathway.

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“…The protein-protein interactions that contribute to control of transcription factor localization and function are mediated by a variety of different structural motifs including the leucine zipper as in the case of cFos and cJun (Landschulz et al, 1988;Turner and Tjian, 1989;Gentz et al, 1989), the helix-loop-helix motif in the case of MyoD and Id (Murre et al, 1989a,b;Benezra et al, 1990), and ankyrin repeats in the case of GABP ot and/~ l.aMarco et ai., 1991) and NF-KB and DcB (Baeuerle and Baltimore, 1988;Hatada et al, 1992). The LIM motif may emerge as yet another protein-interactive domain that is utilized in transcriptional regulation.…”

Section: Functional Implicationsmentioning

confidence: 99%

Zyxin and cCRP: two interactive LIM domain proteins associated with the cytoskeleton.

Sadler

Crawford

Michelsen

et al. 1992

The Journal of Cell Biology

335

247

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Abstract. Interaction with extraceUular matrix can trigger a variety of responses by cells including changes in specific gene expression and cell differentiation. The mechanism by which cell surface events are coupled to the transcriptional machinery is not understood, however, proteins localized at sites of cell-substratum contact are likely to function as signal transducers. We have recently purified and characterized a low abundance adhesion plaque protein called zyxin (Crawford, A. W., and M. C. Beckerle. 1991. J. Biol. Chem. 266:5847-5853; Crawford, A. W., J. W. Michelsen, and M. C. Beckerle. 1992. J. Cell Biol. 116:1381-1393. We have now isolated and sequenced zyxin cDNA and we report here that zyxin exhibits an unusual proline-rich NH2-terminus followed by three tandemly arrayed LIM domains. LIM domains have previously been identified in proteins that play important roles in transcriptional regulation and cellular differentiation. LIM domains have been proposed to coordinate metal ions and we have demonstrated by atomic absorption spectroscopy that purified zyxin binds zinc, a result consistent with the idea that zyxin has zinc fingers. In addition, we have discovered that zyxin interacts in vitro with a 23-kD protein that also exhibits LIM domains. Microsequence analysis has revealed that the 23-kD protein (or cCRP) is the chicken homologue of the human cysteine-rich protein (hCRP). By double-label indirect immunofluorescence, we found that zyxin and cCRP are extensively colocalized in chicken embryo fibroblasts, consistent with the idea that they interact in vivo. We conclude that LIM domains are zinc-binding sequences that may be involved in protein-protein interactions. The demonstration that two cytoskeletal proteins, zyxin and cCRP, share a sequence motif with proteins important for transcriptional regulation raises the possibility that zyxin and cCRP are components of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression.

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Parallel Association of Fos and Jun Leucine Zippers Juxtaposes DNA Binding Domains

Cited by 568 publications

References 30 publications

A novel tumour associated leucine zipper protein targeting to sites of gene transcription and splicing

A novel tumour associated leucine zipper protein targeting to sites of gene transcription and splicing

Analysis of the SIP3 protein identified in a two-hybrid screen for interaction with the SNF1 protein kinase

Zyxin and cCRP: two interactive LIM domain proteins associated with the cytoskeleton.

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