RLIM inhibits functional activity of LIM homeodomain transcription factors via recruitment of the histone deacetylase complex

@article{Bach1999RLIMIF,
  title={RLIM inhibits functional activity of LIM homeodomain transcription factors via recruitment of the histone deacetylase complex},
  author={Ingolf Bach and Concepci{\'o}n Rodr{\'i}guez-Esteban and Catherine Carri{\`e}re and Anil Bhushan and Anna Krones and David W. Rose and Christopher K. Glass and Bogi Andersen and Juan Carlos Izpisua Belmonte and Michael G. Rosenfeld},
  journal={Nature Genetics},
  year={1999},
  volume={22},
  pages={394-399}
}
LIM domains are required for both inhibitory effects on LIM homeodomain transcription factors and synergistic transcriptional activation events. The inhibitory actions of the LIM domain can often be overcome by the LIM co-regulator known as CLIM2, LDB1 and NLI (referred to hereafter as CLIM2; refs 2, 3, 4). The association of the CLIM cofactors with LIM domains does not, however, improve the DNA-binding ability of LIM homeodomain proteins, suggesting the action of a LIM-associated inhibitor… 

Figures from this paper

Ubiquitination-dependent cofactor exchange on LIM homeodomain transcription factors
TLDR
RLIM is identified as a ubiquitin protein ligase that is able to target CLIM cofactors for degradation through the 26S proteasome pathway and is demonstrated to provide a mechanistic basis for cofactor exchange on DNA-bound transcription factors.
p53 Represses Transcription of RING Finger LIM Domain-Binding Protein RLIM through Sp1
TLDR
The results provided data to enlarge the knowledge of transcriptional regulation of RLIM and suggested a new pathway by which physiological and pathological activators of p53 may affect development.
Proteasomal selection of multiprotein complexes recruited by LIM homeodomain transcription factors
TLDR
This work identifies a cascade of specific protein interactions that protect LIM-HD multiprotein complexes from proteasomal degradation, and shows that stabilizing cofactors prevent binding of ubiquitin ligases to multiple protein interaction domains in LIM- HD recruited protein complexes.
The Ajuba LIM domain protein is a corepressor for SNAG domain mediated repression and participates in nucleocytoplasmic Shuttling.
TLDR
SNAG domain proteins may bind Ajuba, trapping it in the nucleus where it functions as an adapter or molecular scaffold for the assembly of macromolecular repression complexes at target promoters, and enhances SNAG-mediated transcriptional repression.
Functional characterization of the gene encoding RLIM, the corepressor of LIM homeodomain factors.
TLDR
Transient cotransfections reveal that the proximal Rnf12 promoter can be activated in vitro by ubiquitously and more restrictively expressed transcription factors, some of which are known mediators of signal transduction pathways, e.g., mammalian Krüppel-like transcription factors and Sox and ets-related proteins.
Requirement of LIM domains for LIM1 function in mouse head development
TLDR
The mutated Lim1 gene is mutated to alter the conserved amino acid residues that are required for zinc finger structure within both of the Lim domains, suggesting that the integrity of the LIM domains is essential for LIM1 activity in mouse head development.
Nucleocytoplasmic Shuttling Mediated Repression and Participates in − Domain The Ajuba LIM Domain Protein Is a Corepressor for SNAG
TLDR
SNAG domain proteins may bind Ajuba, trapping it in the nucleus where it functions as an adapter or molecular scaffold for the assembly of macromolecular repression complexes at target promoters, and enhances SNAG-mediated transcriptional repression.
Dynamic expression of LIM cofactors in the developing mouse neural tube
TLDR
The dynamic expression of cofactors participating in the regulation of LIM‐HD proteins during the development of the neural tube in mice is demonstrated and additional post‐transcriptional regulation in the nuclear LIM‐ HD protein network is suggested.
Multiple functions of LIM domain-binding CLIM/NLI/Ldb cofactors during zebrafish development
Regulation of estrogen-dependent transcription by the LIM cofactors CLIM and RLIM in breast cancer.
TLDR
Results from a human breast cancer tissue microarray of 1,335 patients revealed a highly significant correlation of elevated CLIM levels to ER/progesterone receptor positivity and poor differentiation of tumors, indicating that LIM cofactors CLIM and RLIM regulate the biological activity of ERalpha during the development of human breast cancers.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 30 REFERENCES
Interactions of the LIM-domain-binding factor Ldbl with LIM homeodomain proteins
TLDR
A new LIM-domain-binding factor is isolated on the basis of its ability to interact with the LIM-HD protein Lhxl (Liml) and high-affinity binding by Ldbl requires paired LIM domains and is restricted to the related subgroup of LIM domains found in LIM- HD and LMO proteins.
A family of LIM domain-associated cofactors confer transcriptional synergism between LIM and Otx homeodomain proteins.
TLDR
This work isolated murine cDNAs encoding two highly homologous proteins that specifically interact with the LIM domains of P-Lim/Lhx3 and several other LIM homeodomain factors and link them to members of the Otx class of transcription factors in gene activation events during embryogenesis via the actions of specific cofactors.
Functional analysis of the nuclear LIM domain interactor NLI
TLDR
NLI contains at least two functionally independent domains and may serve as a negative regulator of synergistic transcriptional responses which require direct interaction via LIM domains, indicating that NLI may regulate the transcriptional activity of LIM homeodomain proteins by determining specific partner interactions.
Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting protein, is expressed early in neuronal development.
TLDR
A novel protein is isolated, nuclear LIM interactor (NLI), that specifically associates with a single LIM domain in all nuclear LIM proteins tested, suggesting the mutual involvement of these proteins in the differentiation process.
Interactions between LIM Domains and the LIM Domain-binding Protein Ldb1*
TLDR
This study localized the transcriptional activation domain of Xlim-1 to its carboxyl-terminal region, and characterized the interactions of the amino-terminally located LIM domains with Ldb1.
A complex containing N-CoR, mSln3 and histone deacetylase mediates transcriptional repression
TLDR
Data predict that the ligand-induced switch of heterodimeric nuclear receptors from repressor to activator functions involves the exchange of complexes containing histone deacetylases with those that have histone acetylase activity.
Ring1A is a transcriptional repressor that interacts with the Polycomb‐M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain
TLDR
The discovery of two murine proteins, Ring1A and Ring1B, that interact directly with the repressor domain of M33 are suggested to contribute to a tissue‐specific function of Pc‐G–protein complexes during mammalian development.
...
1
2
3
...