GoPubMed Proteins lists recent and important papers and reviews for
proteins. Page last changed on 14 Mar 2013.
LIM domain binding 1
Ldb1, NLI, CLIM2
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Papers on
Ldb1
Structural basis of the interaction of the breast cancer oncogene LMO4 with the tumour suppressor CtIP/RBBP8.
New
Sydney, Australia. In J Mol Biol, 23 Feb 2013
Our data reveal that CtIP and the essential LMO-cofactor LDB1 bind to the same face on LMO4 and cannot simultaneously bind to LMO4.
Role of transcriptional corepressor ETO2 in erythroid cells.
New
Sendai, Japan. In Exp Hematol, Dec 2012
Transcriptional corepressor ETO2 is a component of a protein complex containing master regulators of hematopoiesis, including GATA-1, SCL/TAL1, LMO2 and LDB1.
Suspected leukemia oncoproteins CREB1 and LYL1 regulate Op18/STMN1 expression.
New
Toronto, Canada. In Biochim Biophys Acta, Nov 2012
NLI, LMO2 and GATA2 are previously described co-activators of Tal1/Lyl1-E47 transcriptional complexes and potentiate Lyl1 activation of the STMN1 promoter while having no effect on TAL1 transactivation.
A novel complex, RUNX1-MYEF2, represses hematopoietic genes in erythroid cells.
New
Rotterdam, Netherlands. In Mol Cell Biol, Oct 2012
RUNX1 has been shown to be part of a large transcription factor complex, together with LDB1, GATA1, TAL1, and ETO2 (N.
Medulloblastoma exome sequencing uncovers subtype-specific somatic mutations.
New
Impact
Cambridge, United States. In Nature, Sep 2012
Recurrent somatic mutations were newly identified in an RNA helicase gene, DDX3X, often concurrent with CTNNB1 mutations, and in the nuclear co-repressor (N-CoR) complex genes GPS2, BCOR and LDB1.
Identification of LMO2 transcriptome and interactome in diffuse large B-cell lymphoma.
New
Miami, United States. In Blood, Jul 2012
In DLBCL, the LMO2 complex contains some of the traditional partners, such as LDB1, E2A, HEB, Lyl1, ETO2, and SP1, but not TAL1 or GATA proteins.
Dynamic long-range chromatin interactions control Myb proto-oncogene transcription during erythroid development.
New
Rotterdam, Netherlands. In Embo J, Mar 2012
We propose a model for Myb activation by distal enhancers dynamically bound by KLF1 and the GATA1/TAL1/LDB1 complex, which primarily function as a transcription elongation element through chromatin looping.
Distinct Ldb1/NLI complexes orchestrate γ-globin repression and reactivation through ETO2 in human adult erythroid cells.
GeneRIF
Bethesda, United States. In Blood, 2012
We investigated NLI (Ldb1 homolog) complex occupancy and chromatin conformation of the beta-globin locus in human erythroid cells.
Structural basis of simultaneous recruitment of the transcriptional regulators LMO2 and FOG1/ZFPM1 by the transcription factor GATA1.
Sydney, Australia. In Proc Natl Acad Sci U S A, 2011
Most GATA1-regulated events require GATA1 to bind FOG1, and essentially all GATA1-activated genes are cooccupied by a TAL1/E2A/LMO2/LDB1 complex; however, it is not known whether FOG1 and TAL1/E2A/LMO2/LDB1 are simultaneously recruited by GATA1.
LMO4 functions as a co-activator of neurogenin 2 in the developing cortex.
Houston, United States. In Development, 2011
LMO4 and its binding partner nuclear LIM interactor (NLI/LDB1/CLIM2) interact with NGN2 simultaneously, forming a multi-protein transcription complex.
Nuclear adaptor Ldb1 regulates a transcriptional program essential for the maintenance of hematopoietic stem cells.
Impact
GeneRIF
Bethesda, United States. In Nat Immunol, 2011
controls transcriptional program required for stem cells maintenance by restricting their differentiation
Liver-specific Ldb1 deletion results in enhanced liver cancer development.
GeneRIF
Mainz, Germany. In J Hepatol, 2010
knockout mice demonstrated a significantly enhanced growth of liver cancer (HCC) by means of tumor size and number, advocating for an essential role of Ldb1 in HCC development
A requirement for Lim domain binding protein 1 in erythropoiesis.
GeneRIF
Bethesda, United States. In J Exp Med, 2010
a role for Ldb1 in erythropoiesis in vivo and establish a critical function for Ldb1-nucleated complexes in regulating the erythroid/megakaryocyte transcriptional program.
Multiple functions of Ldb1 required for beta-globin activation during erythroid differentiation.
GeneRIF
Bethesda, United States. In Blood, 2010
Ldb1 stabilizes its erythroid complex partners on beta-globin chromatin, even though it is not one of the DNA-binding components. In addition, Ldb1 is necessary for enrichment of key transcriptional components in the locus.
Decoding the LIM development code.
Review
In Trans Am Clin Climatol Assoc, 2002
The basic code is a homotetramer of 2 LIM homeodomain proteins bridged by the adaptor protein, nuclear LIM interactor (NLI).
A short history of LIM domains (1993-2002): from protein interaction to degradation.
Review
Gif-sur-Yvette, France. In Mol Neurobiol, 2002
In this review, the authors describe the progressive discoveries of NLI/Ldb/CLIM, LMO and RLIM, and discuss how the field was very recently updated by the finding that LIM-hd transcriptional activity is controlled by regulated degradation of cofactors and LIM-hd themselves.
LIM factor Lhx3 contributes to the specification of motor neuron and interneuron identity through cell-type-specific protein-protein interactions.
Impact
Los Angeles, United States. In Cell, 2002
Using in vivo function and protein interaction assays, we found that Lhx3 binds directly to the LIM cofactor NLI to trigger V2 interneuron differentiation.
Ubiquitination-dependent cofactor exchange on LIM homeodomain transcription factors.
Impact
Hamburg, Germany. In Nature, 2002
LIM homeodomain (LIM-HD) transcription factors associate with RLIM (RING finger LIM domain-binding protein) and with CLIM (cofactor of LIM-HD proteins; also known as NLI, Ldb and Chip) cofactors.
RLIM inhibits functional activity of LIM homeodomain transcription factors via recruitment of the histone deacetylase complex.
Impact
San Diego, United States. In Nat Genet, 1999
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 2-4).
