scholarly journals Intracellular Enhancement of BMP Signaling by LIM-Domain Protein FHL3 Controls Spatiotemporal Emergence of the Neural Crest Driven by WNT Signaling

2020 ◽  
Author(s):  
Mansour Alkobtawi ◽  
Patrick Pla ◽  
Anne Monsoro-Burq
Keyword(s):  
Wnt Signaling ◽  
Neural Crest ◽  
Bmp Signaling ◽  
Lim Domain ◽  
Lim Domain Protein ◽  
Domain Protein

scholarly journals Intracellular enhancement of BMP signaling by LIM-domain protein FHL3 controls spatiotemporal emergence of the neural crest driven by WNT signaling

2019 ◽  
Author(s):  
Mansour Alkobtawi ◽  
Patrick Pla ◽  
Anne H. Monsoro-Burq
Keyword(s):  
Wnt Signaling ◽  
Neural Crest ◽  
Bmp Signaling ◽  
Paraxial Mesoderm ◽  
List Type ◽  
Lim Domain ◽  
Neural Crest Development ◽  
Lim Domain Protein ◽  
Smad Phosphorylation ◽  
Domain Protein

AbstractHow multiple morphogen signals are coordinated in space and time to position key embryonic tissues remains elusive. During neural crest formation, bone morphogenetic protein (BMP), fibroblast growth factor (FGF) and WNT signaling cooperate by acting either on the paraxial mesoderm or directly on the neural border ectoderm, but how each tissue interprets this complex information remains poorly understood. Here we show that Fhl3, a scaffold LIM domain protein of previously unknown developmental function, is essential for neural crest formation by linking BMP and WNT signaling thereby positioning the neural crest-inducing signaling center in the paraxial mesoderm. During gastrulation, Fhl3 promotes Smad phosphorylation and Smad-dependent wnt8 activation specifically in the paraxial mesoderm, thus modifying the respective mesoderm or ectoderm cell response to the extracellular BMP gradient. This ensures neural border ectoderm specification by the underlying mesoderm via non-cell autonomous WNT signaling. During neurulation, neural crest inducers activate fhl3, promoting BMP/Smad-dependent WNT activity required for neural crest specification. Our findings highlight how Fhl3, acting cell-autonomously, ensures a fine spatial, temporal and germ layer-specific coordination of BMP and WNT signaling at several steps of neural crest development.Highlights:-FHL3 is a novel intracellular enhancer of BMP signaling during early development.-FHL3 ensures cross-talk between BMP and WNT signaling by Smad1-dependent wnt8 activation in the paraxial mesoderm.-FHL3 reiterated function in paraxial mesoderm and in neural border ectoderm is essential for neural crest development at the border of the neural plate.

Proteomic identification of the LIM domain protein FHL1 as the gene-product mutated in reducing body myopathy

2009 ◽  
Vol 40 (01) ◽  
Author(s):  
J Schessl ◽  
Y Zou ◽  
MJ McGrath ◽  
BS Cowling ◽  
B Maiti ◽  
...  
Keyword(s):  
Gene Product ◽  
Lim Domain ◽  
Lim Domain Protein ◽  
Proteomic Identification ◽  
Domain Protein

scholarly journals Four-and-a-half LIM domain protein 2 (FHL2) deficiency protects mice from diet-induced obesity and high FHL2 expression marks human obesity

Metabolism ◽  
2021 ◽  
pp. 154815
Author(s):  
Maria P. Clemente-Olivo ◽  
Jayron J. Habibe ◽  
Mariska Vos ◽  
Roelof Ottenhoff ◽  
Aldo Jongejan ◽  
...  
Keyword(s):  
Lim Domain ◽  
Human Obesity ◽  
Diet Induced Obesity ◽  
Lim Domain Protein ◽  
Domain Protein

scholarly journals The LIM domain protein nTRIP6 modulates the dynamics of myogenic differentiation

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Tannaz Norizadeh Abbariki ◽  
Zita Gonda ◽  
Denise Kemler ◽  
Pavel Urbanek ◽  
Tabea Wagner ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Satellite Cells ◽  
Muscle Regeneration ◽  
Myogenic Differentiation ◽  
Skeletal Muscle Regeneration ◽  
Temporal Control ◽  
Lim Domain ◽  
Lim Domain Protein ◽  
Domain Protein

AbstractThe process of myogenesis which operates during skeletal muscle regeneration involves the activation of muscle stem cells, the so-called satellite cells. These then give rise to proliferating progenitors, the myoblasts which subsequently exit the cell cycle and differentiate into committed precursors, the myocytes. Ultimately, the fusion of myocytes leads to myofiber formation. Here we reveal a role for the transcriptional co-regulator nTRIP6, the nuclear isoform of the LIM-domain protein TRIP6, in the temporal control of myogenesis. In an in vitro model of myogenesis, the expression of nTRIP6 is transiently up-regulated at the transition between proliferation and differentiation, whereas that of the cytosolic isoform TRIP6 is not altered. Selectively blocking nTRIP6 function results in accelerated early differentiation followed by deregulated late differentiation and fusion. Thus, the transient increase in nTRIP6 expression appears to prevent premature differentiation. Accordingly, knocking out the Trip6 gene in satellite cells leads to deregulated skeletal muscle regeneration dynamics in the mouse. Thus, dynamic changes in nTRIP6 expression contributes to the temporal control of myogenesis.

Chromosomal mapping, tissue distribution and cDNA sequence of Four-and-a-half LIM domain protein 1 (FHL1)

Gene ◽  
1998 ◽  
Vol 216 (1) ◽  
pp. 163-170 ◽  
Author(s):  
Simon Ming Yuen Lee ◽  
Stephen Kwok Wing Tsui ◽  
Kwok Keung Chan ◽  
Merce Garcia-Barcelo ◽  
Mary Miu Yee Waye ◽  
...  
Keyword(s):  
Tissue Distribution ◽  
Cdna Sequence ◽  
Chromosomal Mapping ◽  
Lim Domain ◽  
Lim Domain Protein ◽  
Domain Protein

scholarly journals The Four-and-a-half LIM Domain Protein 2 Regulates Vascular Smooth Muscle Phenotype and Vascular Tone

2009 ◽  
Vol 284 (19) ◽  
pp. 13202-13212 ◽  
Author(s):  
Nicole A. Neuman ◽  
Susan Ma ◽  
Gavin R. Schnitzler ◽  
Yan Zhu ◽  
Giorgio Lagna ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Vascular Tone ◽  
Lim Domain ◽  
Lim Domain Protein ◽  
Domain Protein

scholarly journals DYC-1, a Protein Functionally Linked to Dystrophin in Caenorhabditis elegans Is Associated with the Dense Body, Where It Interacts with the Muscle LIM Domain Protein ZYX-1

2008 ◽  
Vol 19 (3) ◽  
pp. 785-796 ◽  
Author(s):  
Claire Lecroisey ◽  
Edwige Martin ◽  
Marie-Christine Mariol ◽  
Laure Granger ◽  
Yannick Schwab ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Dense Body ◽  
Striated Muscles ◽  
Lim Domain ◽  
Functional Link ◽  
C Elegans ◽  
Lim Domain Protein ◽  
Muscle Necrosis ◽  
Domain Protein

In Caenorhabditis elegans, mutations of the dystrophin homologue, dys-1, produce a peculiar behavioral phenotype (hyperactivity and a tendency to hypercontract). In a sensitized genetic background, dys-1 mutations also lead to muscle necrosis. The dyc-1 gene was previously identified in a genetic screen because its mutation leads to the same phenotype as dys-1, suggesting that the two genes are functionally linked. Here, we report the detailed characterization of the dyc-1 gene. dyc-1 encodes two isoforms, which are expressed in neurons and muscles. Isoform-specific RNAi experiments show that the absence of the muscle isoform, and not that of the neuronal isoform, is responsible for the dyc-1 mutant phenotype. In the sarcomere, the DYC-1 protein is localized at the edges of the dense body, the nematode muscle adhesion structure where actin filaments are anchored and linked to the sarcolemma. In yeast two-hybrid assays, DYC-1 interacts with ZYX-1, the homologue of the vertebrate focal adhesion LIM domain protein zyxin. ZYX-1 localizes at dense bodies and M-lines as well as in the nucleus of C. elegans striated muscles. The DYC-1 protein possesses a highly conserved 19 amino acid sequence, which is involved in the interaction with ZYX-1 and which is sufficient for addressing DYC-1 to the dense body. Altogether our findings indicate that DYC-1 may be involved in dense body function and stability. This, taken together with the functional link between the C. elegans DYC-1 and DYS-1 proteins, furthermore suggests a requirement of dystrophin function at this structure. As the dense body shares functional similarity with both the vertebrate Z-disk and the costamere, we therefore postulate that disruption of muscle cell adhesion structures might be the primary event of muscle degeneration occurring in the absence of dystrophin, in C. elegans as well as vertebrates.

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