Interactions of the LIM-domain-binding factor Ldbl with LIM homeodomain proteins

Nature ◽  
1996 ◽  
Vol 384 (6606) ◽  
pp. 270-272 ◽  
Author(s):  
Alan D. Agulnick ◽  
Masanori Taira ◽  
Joseph J. Breen ◽  
Tomohiro Tanaka ◽  
Igor B. Dawid ◽  
...  
Keyword(s):  
Lim Domain ◽  
Homeodomain Proteins ◽  
Binding Factor ◽  
Lim Homeodomain

Differential expression of a transcription regulatory factor, the LIM domain only 4 protein Lmo4, in muscle sensory neurons

Development ◽  
2002 ◽  
Vol 129 (21) ◽  
pp. 4879-4889
Author(s):  
Hsiao-Huei Chen ◽  
Joseph W. Yip ◽  
Alexandre F. R. Stewart ◽  
Eric Frank
Keyword(s):  
Differential Expression ◽  
Sensory Neurons ◽  
Molecular Mechanisms ◽  
Neuronal Development ◽  
Expression Patterns ◽  
Cdna Libraries ◽  
Homeodomain Protein ◽  
Lim Domain ◽  
Homeodomain Proteins ◽  
Lim Homeodomain

In the stretch-reflex system, proprioceptive sensory neurons make selective synaptic connections with different subsets of motoneurons, according to the peripheral muscles they supply. To examine the molecular mechanisms that may influence the selection of these synaptic targets, we constructed single-cell cDNA libraries from sensory neurons that innervate antagonist muscles. Differential screening of these libraries identified a transcription regulatory co-factor of the LIM homeodomain proteins, the LIM domain only 4 protein Lmo4, expressed in most adductor but few sartorius sensory neurons. Differential patterns of Lmo4 expression were also seen in sensory neurons supplying three other muscles. A subset of motoneurons also expresses Lmo4 but the pattern of expression is not specific for motor pools. Differential expression of Lmo4 occurs early, as neurons develop their characteristic LIM homeodomain protein expression patterns. Moreover, ablation of limb buds does not block Lmo4 expression, suggesting that an intrinsic program controls the early differential expression of Lmo4. LIM homeodomain proteins are known to regulate several aspects of sensory and motor neuronal development. Our results suggest that Lmo4 may participate in this differentiation by regulating the transcriptional activity of LIM homeodomain proteins.

scholarly journals Structural Basis for Partial Redundancy in a Class of Transcription Factors, the LIM Homeodomain Proteins, in Neural Cell Type Specification

2011 ◽  
Vol 286 (50) ◽  
pp. 42971-42980 ◽  
Author(s):  
Morgan S. Gadd ◽  
Mugdha Bhati ◽  
Cy M. Jeffries ◽  
David B. Langley ◽  
Jill Trewhella ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Neural Cell ◽  
Structural Basis ◽  
Cell Type ◽  
Homeodomain Proteins ◽  
Partial Redundancy ◽  
Type Specification ◽  
Lim Homeodomain

scholarly journals The transcriptional co-factor Chip acts with LIM-homeodomain proteins to set the boundary of the eye field inDrosophila

Development ◽  
2009 ◽  
Vol 137 (2) ◽  
pp. 273-281 ◽  
Author(s):  
Jean-Yves Roignant ◽  
Kevin Legent ◽  
Florence Janody ◽  
Jessica E. Treisman
Keyword(s):  
Homeodomain Proteins ◽  
Eye Field ◽  
Lim Homeodomain

scholarly journals Functional analysis of the nuclear LIM domain interactor NLI.

1997 ◽  
Vol 17 (10) ◽  
pp. 5688-5698 ◽  
Author(s):  
L W Jurata ◽  
G N Gill
Keyword(s):  
Transcriptional Activation ◽  
Negative Regulator ◽  
Homeodomain Protein ◽  
Lim Domain ◽  
Transcriptional Responses ◽  
Amino Terminal ◽  
High Affinity ◽  
Lim Domains ◽  
Lim Homeodomain

LIM homeodomain and LIM-only (LMO) transcription factors contain two tandemly arranged Zn2+-binding LIM domains capable of mediating protein-protein interactions. These factors have restricted patterns of expression, are found in invertebrates as well as vertebrates, and are required for cell type specification in a variety of developing tissues. A recently identified, widely expressed protein, NLI, binds with high affinity to the LIM domains of LIM homeodomain and LMO proteins in vitro and in vivo. In this study, a 38-amino-acid fragment of NLI was found to be sufficient for the association of NLI with nuclear LIM domains. In addition, NLI was shown to form high affinity homodimers through the amino-terminal 200 amino acids, but dimerization of NLI was not required for association with the LIM homeodomain protein Lmxl. Chemical cross-linking analysis revealed higher-order complexes containing multiple NLI molecules bound to Lmx1, indicating that dimerization of NLI does not interfere with LIM domain interactions. Additionally, NLI formed complexes with Lmx1 on the rat insulin I promoter and inhibited the LIM domain-dependent synergistic transcriptional activation by Lmx1 and the basic helix-loop-helix protein E47 from the rat insulin I minienhancer. These studies indicate that 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. Thus, NLI may regulate the transcriptional activity of LIM homeodomain proteins by determining specific partner interactions.

scholarly journals GATA2-Induced Silencing and LIM-Homeodomain Protein-Induced Activation Are Mediated by a Bi-Functional Response Element in the Rat GnRH Receptor Gene

2013 ◽  
Vol 27 (1) ◽  
pp. 74-91 ◽  
Author(s):  
Anne-Laure Schang ◽  
Anne Granger ◽  
Bruno Quérat ◽  
Christian Bleux ◽  
Joëlle Cohen-Tannoudji ◽  
...  
Keyword(s):  
Cell Fate ◽  
Promoter Activity ◽  
Receptor Gene ◽  
Gnrh Receptor ◽  
Expression Vectors ◽  
Homeodomain Protein ◽  
Homeodomain Proteins ◽  
Enhancer Activity ◽  
Response Element ◽  
Lim Homeodomain

GATA2 transcription factor and LIM homeodomain proteins Islet1 (ISL1) and LIM homeobox 3 (LHX3) are suspected to be involved in gonadotrope cell fate and maintenance. The GnRH receptor gene (Gnrhr), crucial for gonadotrope function, is expressed in the pituitary gland from embryonic day 13.5 onward, well before LH and FSH β-subunits. This expression pattern together with the presence of WGATAR and TAAT motifs in Gnrhr promoter sequences suggests the involvement of early transcription factors in promoter activation. In this study, using a well-characterized transgenic mouse model, GATA2 was found colocalized with Gnrhr promoter activity in the pituitary. Transient transfection of Gnrhr promoter luciferase fusion constructs together with either GATA2 expression vectors or small interfering RNA in gonadotrope cell lines indicated that GATA2, which typically acts as a trans-activator, unexpectedly repressed Gnrhr promoter activity. Using DNA chromatography affinity and EMSA, we demonstrated that GATA2 operates via a response element containing a peculiar palindromic GATA motif that overlaps a critical TAAT motif involved in LHX3/ISL1 trans-activation. Indeed, despite the inhibitory action of GATA2, this element displayed a clear-cut enhancer activity in gonadotrope cells. Chromatin immunoprecipitation assays indicated that GATA2, LHX3, and ISL1 interact with a Gnrhr promoter fragment encompassing this element. The trans-repressive action of GATA2 on Gnrhr promoter activity is likely balanced or even hindered by trans-activating effects of LIM homeodomain proteins via this novel bifunctional LIM/GATA response element. Such a hierarchical interplay may contribute to finely adjust Gnrhr gene expression in gonadotrope cell lineage during pituitary development as well as in the adult animal.

scholarly journals A Postmitotic Role for Isl-Class LIM Homeodomain Proteins in the Assignment of Visceral Spinal Motor Neuron Identity

Neuron ◽  
2004 ◽  
Vol 41 (3) ◽  
pp. 337-350 ◽  
Author(s):  
Joshua P Thaler ◽  
Sonya J Koo ◽  
Artur Kania ◽  
Karen Lettieri ◽  
Shane Andrews ◽  
...  
Keyword(s):  
Motor Neuron ◽  
Homeodomain Proteins ◽  
Spinal Motor Neuron ◽  
Spinal Motor ◽  
Lim Homeodomain
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