Genomic structure, alternative transcripts and chromosome location of the human LIM domain binding protein 1 gene LDB1

1999 ◽  
Vol 87 (1-2) ◽  
pp. 119-124 ◽  
Author(s):  
M. Drechsler ◽  
V. Schumacher ◽  
S. Friedrich ◽  
G. Wildhardt ◽  
S. Giesler ◽  
...  
Keyword(s):  
Binding Protein ◽  
Genomic Structure ◽  
Chromosome Location ◽  
Lim Domain ◽  
Alternative Transcripts

scholarly journals Genomic Structure and Chromosomal Localization of the Mouse LIM Domain-Binding Protein 1 Gene,Ldb1

Genomics ◽  
1998 ◽  
Vol 48 (1) ◽  
pp. 87-92 ◽  
Author(s):  
Tsuyoshi Yamashita ◽  
Alan D. Agulnick ◽  
Neal G. Copeland ◽  
Debra J. Gilbert ◽  
Nancy A. Jenkins ◽  
...  
Keyword(s):  
Chromosomal Localization ◽  
Binding Protein ◽  
Genomic Structure ◽  
Lim Domain

Role of the LIM domain binding protein LDB1 and the LIM only factor LMO4 in SHH subgroup medulloblastoma

2014 ◽  
Vol 226 (03) ◽  
Author(s):  
S Hutter ◽  
PA Northcott ◽  
M Kool ◽  
SM Pfister ◽  
D Kawauchi ◽  
...  
Keyword(s):  
Binding Protein ◽  
Lim Domain

Genomic structure, chromosome location, and alternative splicing of the humanNKG2A gene

1996 ◽  
Vol 44 (4) ◽  
pp. 286-291 ◽  
Author(s):  
Béatrice Plougastel ◽  
Tania Jones ◽  
John Trowsdale
Keyword(s):  
Alternative Splicing ◽  
Genomic Structure ◽  
Chromosome Location

scholarly journals Rotational symmetry of the structured Chip/LDB-SSDP core module of the Wnt enhanceosome

2019 ◽  
Vol 116 (42) ◽  
pp. 20977-20983 ◽  
Author(s):  
Miha Renko ◽  
Marc Fiedler ◽  
Trevor J. Rutherford ◽  
Jonas V. Schaefer ◽  
Andreas Plückthun ◽  
...  
Keyword(s):  
Cell Fate ◽  
Structural Model ◽  
Mutational Analysis ◽  
Binding Protein ◽  
Rotational Symmetry ◽  
Lim Domain ◽  
Animal Cells ◽  
Developmental Control ◽  
Cell Fate Decisions ◽  
Core Module

The Chip/LIM-domain binding protein (LDB)–single-stranded DNA-binding protein (SSDP) (ChiLS) complex controls numerous cell-fate decisions in animal cells, by mediating transcription of developmental control genes via remote enhancers. ChiLS is recruited to these enhancers by lineage-specific LIM-domain proteins that bind to its Chip/LDB subunit. ChiLS recently emerged as the core module of the Wnt enhanceosome, a multiprotein complex that primes developmental control genes for timely Wnt responses. ChiLS binds to NPFxD motifs within Pygopus (Pygo) and the Osa/ARID1A subunit of the BAF chromatin remodeling complex, which could synergize with LIM proteins in tethering ChiLS to enhancers. Chip/LDB and SSDP both contain N-terminal dimerization domains that constitute the bulk of their structured cores. Here, we report the crystal structures of these dimerization domains, in part aided by DARPin chaperones. We conducted systematic surface scanning by structure-designed mutations, followed by in vitro and in vivo binding assays, to determine conserved surface residues required for binding between Chip/LDB, SSDP, and Pygo-NPFxD. Based on this, and on the 4:2 (SSDP-Chip/LDB) stoichiometry of ChiLS, we derive a highly constrained structural model for this complex, which adopts a rotationally symmetrical SSDP2-LDB2-SSDP2 architecture. Integrity of ChiLS is essential for Pygo binding, and our mutational analysis places the NPFxD pockets on either side of the Chip/LDB dimer, each flanked by an SSDP dimer. The symmetry and multivalency of ChiLS underpin its function as an enhancer module integrating Wnt signals with lineage-specific factors to operate context-dependent transcriptional switches that are pivotal for normal development and cancer.

Genomic Structure and Chromosome Location of the Human mutT Homologue Gene MTH1 Encoding 8-Oxo-dGTPase for Prevention of A:T to C:G Transversion

Genomics ◽  
1994 ◽  
Vol 24 (3) ◽  
pp. 485-490 ◽  
Author(s):  
Masato Furuichi ◽  
Michihiro C. Yoshida ◽  
Hisanobu Oda ◽  
Tatsurou Tajiri ◽  
Yusaku Nakabeppu ◽  
...  
Keyword(s):  
Genomic Structure ◽  
Chromosome Location

Single-Stranded DNA-Binding Proteins (SSBPs) Promote the Oligomerization of LIM-Domain Binding Protein Ldb1

Blood ◽  
2008 ◽  
Vol 112 (11) ◽  
pp. 2437-2437
Author(s):  
Ying Cai ◽  
Lalitha Nagarajan ◽  
Stephen J. Brandt
Keyword(s):  
Dna Binding ◽  
Fusion Proteins ◽  
Mammalian Cells ◽  
Binding Protein ◽  
Binding Activity ◽  
Luciferase Reporter ◽  
Lim Domain ◽  
Single Stranded Dna ◽  
Dna Binding Activity ◽  
E Box

Abstract The multifunctional LIM domain-binding protein Ldb1 is important in multiple developmental programs, including hematopoiesis. An evolutionarily conserved family of proteins with single-stranded DNA-binding activity, the SSBPs, has been shown to act as Ldb1 partners and augment its biological actions. We recently established that Ssbp2 and Ssbp3 were components of an E-box-GATA DNA-binding complex in murine erythroid progenitors containing the LIM-only protein Lmo2 and transcription factors Tal1, E2A, and Gata1 and showed these SSBPs stimulated E box-GATA DNA-binding activity and inhibited Ldb1 ubiquitination and subsequent proteasomal degradation (Genes & Dev.21:942–955, 2007). As its SSBP interaction domain (Ldb1/Chip conserved domain or LCCD) is adjacent to Ldb1’s N-terminal dimerization domain (DD), we sought to determine whether SSBP binding affected Ldb1 dimerization. To investigate, the Ldb1 coding region was fused to the DNA-binding domain of the yeast transcription factor GAL4 (GAL4DBD) and in a second construct to the activation domain of herpesvirus VP16 (VP16AD). These fusion proteins were then expressed in mammalian cells with a luciferase reporter linked to a promoter with iterated GAL4 binding sites. Luciferase activity became detectable with coexpression of the VP16AD-Ldb1 and GAL4DBD-Ldb1 fusions, presumably from Ldb1 dimerization, which increased markedly with simultaneous expression of SSBP2. In contrast, SSBP2 (ΔLUFS) and Ldb1 (ΔLCCD) mutants incapable of interacting with Ldb1 and SSBPs, respectively, were inactive, suggesting that SSBP2 augmentation of Ldb1 dimerization involved direct protein-protein interactions. To exclude an effect of SSBP2 on turnover of Ldb1 fusion proteins, radiolabeled full-length Ldb1 and SSBP3 were prepared by in vitro transcription/translation, mixed, and subjected to chemical crosslinking. Addition of the crosslinker bis(sulfosuccinimidyl)-suberate (BS3) to Ldb1, but not SSBP3, led to the appearance of a radiolabeled protein with mobility in denaturing polyacrylamide gels approximately twice that of Ldb1, consistent with an Ldb1 homodimer. When SSBP3 and Ldb1 were mixed together and crosslinked, a dose-related increase was noted in a more retarded species predicted to contain two molecules each of Ldb1 and SSBP3, together with a decrease in monomeric Ldb1. Finally, two well-characterized dimerization-defective Ldb1 mutants, Ldb1(200–375) and Ldb1(50–375), failed to support the formation of the higher molecular weight species or to homodimerize. Thus, the SSBPs promoted assembly of ternary complexes incorporating both SSBP and Ldb1 in a manner dependent on Ldb1 dimerization. The failure to observe Ldb1-SSBP heterodimers in cross-linking experiments suggests, further, that the SSBPs interacted with preformed Ldb1 dimers. In summary, either through an allosteric effect on Ldb1’s DD or by altering the equilibrium between monomeric and dimeric species, the SSBPs promote Ldb1 oligomerization. Together with inhibition of Ldb1 ubiquitination and turnover, this would serve to augment Ldb1 function.

scholarly journals The LIM domain binding protein 1, Ldb1, has distinct roles in Neu-induced mammary tumorigenesis

2018 ◽  
Vol 1865 (11) ◽  
pp. 1590-1597
Author(s):  
Sarra Ahmed ◽  
Benjamin R. Pryce ◽  
Khalid N. Al-Zahrani ◽  
Luc A. Sabourin
Keyword(s):  
Binding Protein ◽  
Mammary Tumorigenesis ◽  
Lim Domain
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