Loading...
*  "LIM Protein Ajuba Participates in the Repression of ATR-Mediated DNA D" by Sampada Kalan
LIM proteins constitute a superfamily characterized by the presence of specialized domains called LIM. LIM domain is a unique double-zinc finger motif found in a variety of proteins and is mainly involved in protein-protein interactions. Previous work has implicated that members of the Zyxin subfamily of LIM proteins, namely TRIP6 and LPP are involved in the repression of the DNA damage response (DDR) at telomeres. We further explore if another member from this family has an influence on DDR prevention in the cells. Here, we describe a novel role for Ajuba, a Zyxin family LIM protein, in repressing inappropriate activation of ATR kinase mediated DDR. We found that depletion of Ajuba led to a decrease in cell proliferation, apparent delay in the cell cycle, accompanied with increased phosphorylation of Retinoblastoma protein (Rb). We detect ...
https://academicworks.cuny.edu/gc_etds/794/
*  A novel role for transcription factor Lmo4 in thymus development through genetic interaction with Cited2. - Radcliffe...
Deletion of the transcriptional modulator Cited2 in the mouse results in embryonic lethality, cardiovascular malformations, adrenal agenesis, cranial ganglia fusion, exencephaly, and left-right patterning defects, all seen with a varying degree of penetrance. The phenotypic heterogeneity, observed on different genetic backgrounds, indicates the existence of both genetic and environmental modifiers. Mice lacking the LIM domain-containing protein Lmo4 share specific phenotypes with Cited2 null embryos, such as embryonic lethality, cranial ganglia fusion, and exencephaly. These shared phenotypes suggested that Lmo4 may be a potential genetic modifier of the Cited2 phenotype. Examination of Lmo4-deficient embryos revealed partially penetrant cardiovascular malformations and hypoplastic thymus. Examination of Lmo4;Cited2 compound mutants indicated that there is a genetic interaction between Cited2 and Lmo4 in control of thymus development. Our data suggest that this may occur, in ...
https://www.rdm.ox.ac.uk/publications/105267
*  The LIM-only protein Lmo2 is a bridging molecule assembling an erythroid, DNA-binding complex which includes the TAL1, E47,...
The LIM-only protein Lmo2, activated by chromosomal translocations in T-cell leukaemias, is normally expressed in haematopoiesis. It interacts with TAL1 and GATA-1 proteins, but the function of the interaction is unexplained. We now show that in erythroid cells Lmo2 forms a novel DNA-binding complex, with GATA-1, TAL1 and E2A, and the recently identified LIM-binding protein Ldb1/NLI. This oligomeric complex binds to a unique, bipartite DNA motif comprising an E-box, CAGGTG, followed approximately 9 bp downstream by a GATA site. In vivo assembly of the DNA-binding complex requires interaction of all five proteins and establishes a transcriptional transactivating complex. These data demonstrate one function for the LIM-binding protein Ldb1 and establish a function for the LIM-only protein Lmo2 as an obligatory component of an oligomeric, DNA-binding complex which may play a role in haematopoiesis.
https://www.rdm.ox.ac.uk/publications/601814
*  LIM Domain Only 4 ELISA Kits | Biocompare.com
Compare LIM Domain Only 4 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and more.
https://www.biocompare.com/pfu/110627/soids/2-233416/Assay_Kit/ELISA_LIM_Domain_Only_4
*  Recombinant Human LIM domain only 3 protein (ab163265)
Buy our Recombinant Human LIM domain only 3 protein. Ab163265 is a full length protein produced in Wheat germ and has been validated in WB, ELISA. Abcam…
http://www.abcam.com/recombinant-human-lim-domain-only-3-protein-ab163265.html
*  LIM Domain Proteins in the Heart | China-Mainland | Sigma-Aldrich
LIM (Lin-1, Isl1, Mec3) domain proteins all contain least one double zinc finger motif (Fig. 1). LIM family proteins contain between one and five LIM domains plus other that have specific functions such as actin-binding, kinases, and nuclear translocation motifs. We are the first to examine 33 LIM proteins (including three that bind to but do not themselves contain LIM domains) that are implicated in either the development of the heart, heart disorders and failure or both.. We then assembled a cellular 'snapshot' of the LIM proteins known to be expressed in the heart that helps explain how mutations in these proteins may play a role in the development of heart failure. Furthermore, we name the complexity of LIM domain protein interactions as ...
https://www.sigmaaldrich.com/china-mainland/zh/technical-documents/articles/biology/lim-domain-proteins-in-the-heart.html
*  Insights into the Molecular Evolution of the PDZ/LIM Family and Identification of a Novel Conserved Protein Motif
The PDZ and LIM domain-containing protein family is encoded by a diverse group of genes whose phylogeny has currently not been analyzed. In mammals, ten genes are found that encode both a PDZ- and one or several LIM-domains. These genes are: ALP, RIL, Elfin (CLP36), Mystique, Enigma (LMP-1), Enigma homologue (ENH), ZASP (Cypher, Oracle), LMO7 and the two LIM domain kinases (LIMK1 and LIMK2). As conventional alignment and phylogenetic procedures of full-length sequences fell short of elucidating the evolutionary history of these genes, we started to analyze the PDZ and LIM domain sequences themselves. Using information from most sequenced eukaryotic lineages, our phylogenetic analysis is based on full-length cDNA-, EST-derived- and genomic- PDZ and LIM domain sequences of over 25 species, ranging from yeast ...
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0000189
*  The LIM protein Ajuba promotes adipogenesis by enhancing PPARγ and p300/CBP interaction. | Sigma-Aldrich
Sigma-Aldrich offers abstracts and full-text articles by [Q Li, H Peng, H Fan, X Zou, Q Liu, Y Zhang, H Xu, Y Chu, C Wang, K Ayyanathan, F J Rauscher, K Zhang, Z Hou].
https://www.sigmaaldrich.com/catalog/papers/26113042
*  Browse our 7 LIM Domain Binding 1 Protein Proteins
Compare & Order LIM Domain Binding 1 Protein Proteins from many different species. Find the right product on antibodies-online.com.
http://www.antibodies-online.com/stem-cell-maintenance-pathway-61/lim-domain-binding-1-protein-protein-33083/
*  Abstract 119: The Scaffolding Protein Enh1 is Essential for the Protein Kinase C or Protein Kinase D-dependent Activation of...
PDZ-LIM proteins form a family of the scaffolding protein essential for both embryonic and post-natal development. ENH1 (PDLIM5) is a PDZ-LIM protein, composed of an N-terminal PDZ domain and 3 LIM domains at the C-terminal end. The enh gene encodes for several splice variants that have opposite functions. ENH1 promotes the cardiomyocytes hypertrophy whereas ENH splice variants lacking LIM domains prevents it. At the molecular level, ENH1 interacts with Protein kinase C (PKC) and Protein Kinase D1 (PKD1) both kinases playing a pivotal role in the pathological remodeling of the heart. In addition, the binding of ENH1's LIM domains to PKC is sufficient to activate the kinase without any stimulation. However, the downstream events of the ENH1-PKC/PKD1 complex remain unknown. PKC and PKD1 are known to phosphorylate the ...
http://circres.ahajournals.org/content/117/Suppl_1/A119
*  LDB3 - Wikipedia
LIM domain binding 3 (LDB3), also known as Z-band alternatively spliced PDZ-motif (ZASP), is a protein which in humans is encoded by the LDB3 gene. ZASP belongs to the Enigma subfamily of proteins and stabilizes the sarcomere (the basic units of muscles) during contraction, through interactions with actin in cardiac and skeletal muscles. Mutations in the ZASP gene has been associated with several muscular diseases. ZASP is a PDZ domain-containing protein. PDZ motifs are modular protein-protein interaction domains consisting of 80-120 amino acid residues. PDZ domain-containing proteins interact with each other in cytoskeletal assembly or with other proteins involved in targeting and clustering of membrane proteins. ZASP interacts with alpha-actinin-2 through its N-terminal PDZ domain and with protein kinase C via its C-terminal ...
https://en.wikipedia.org/wiki/LDB3
*  The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity.
There are three prolyl hydroxylases (PHD1, 2 and 3) that regulate the hypoxia-inducible factors (HIFs), the master transcriptional regulators that respond to changes in intracellular O(2) tension. In high O(2) tension (normoxia) the PHDs hydroxylate two conserved proline residues on HIF-1α, which leads to binding of the von Hippel-Lindau (VHL) tumour suppressor, the recognition component of a ubiquitin-ligase complex, initiating HIF-1α ubiquitylation and degradation. However, it is not known whether PHDs and VHL act separately to exert their enzymatic activities on HIF-1α or as a multiprotein complex. Here we show that the tumour suppressor protein LIMD1 (LIM domain-containing protein) acts as a molecular scaffold, simultaneously binding the PHDs and VHL, thereby assembling a PHD-LIMD1-VHL protein complex and creating an enzymatic niche that enables efficient degradation of HIF-1α. Depletion of endogenous LIMD1 increases ...
https://qmro.qmul.ac.uk/xmlui/handle/123456789/14130
*  LMO4 - LIM domain only 4 - Gallus gallus (Chicken) - LMO4 gene & protein
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
http://www.uniprot.org/uniprot/Q8JH76
*  Going Out on a LIM and Cysteine-Rich Domains 1 Limb | Hypertension
Hypertension induces cardiac myocytes in the left ventricle to activate a hypertrophic response that involves the upregulation of contractile proteins and the re-expression of fetal genes.1 Transcriptional induction is an important component of this response, and the zinc finger-containing transcription factors GATA4 and GATA6 have been shown to directly stimulate cardiac hypertrophy.2 LIM domain proteins (named after the first 3 LIM proteins identified: Lin11, Isl-1, and Mec-3) interact with transcriptional regulators, kinases, and structural proteins. Because of these protein-protein interactions, LIM domain proteins have been assigned roles in cell growth, differentiation, and cytoskeletal remodeling.3 Several LIM proteins have been identified by proteomic and functional screens of left ventricles ...
http://hyper.ahajournals.org/content/55/2/231
*  Mechanotransduction in Cardiac Hypertrophy and Failure | Circulation Research
Figure 1. A schematic representation of the specific protein complexes linked to sarcomere-mediated mechanotransduction and mechanotransmission in cardiac muscle. CnA indicates calcineurin A; CS-1, calsarcin-1; ECM, extracellullar matrix; ERK2, extracellular signal-regulated kinase-2; FHL1, four-and-a-half LIM domain protein 1; MARPs, muscle-specific ankyrin repeat proteins; MEK2, mitogen-activated protein kinase kinase-2; MLP, muscle-specific LIM domain protein; MURFs, muscle-specific RING-finger proteins; NBR1 indicates neighbor to BRCA1; N-RAP, nebulin-related anchoring protein; p62/SQSTM1, p62/sequestosome-1; PICOT, protein kinase C-interacting cousin of thioredoxin; RAF1, rapid accelerated fibrosarcoma-1; and TCAP, titin Cap (illustration credit: Ben Smith).. ...
http://circres.ahajournals.org/content/116/8/1462.figures-only
*  Structure of the leukemia oncogene LMO2: implications for the assembly of a hematopoietic transcription factor complex :...
The LIM only protein 2 (LMO2) is a key regulator of hematopoietic stem cell development whose ectopic expression in T cells leads to the onset of acute lymphoblastic leukemia. Through its LIM domains, LMO2 is thought to function as the scaffold for a DNA-binding transcription regulator complex, including the basic helix-loop-helix proteins SCL/TAL1 and E47, the zinc finger protein GATA-1, and LIM-domain interacting protein LDB1. To understand the role of LMO2 in the formation of this complex and ultimately to dissect its function in normal and aberrant hematopoiesis, we solved the crystal structure of LMO2 in complex with the LID domain of LDB1 at 2.4 Å resolution. We observe a largely unstructured LMO2 kept in register by the LID binding both LIM domains. Comparison of independently determined crystal structures of LMO2 reveals large movements around a ...
http://sro.sussex.ac.uk/53721/
*  Abstract 791: Cardiac Dysfunction and Heart Failure are Associated with Decreased Levels of Non-Nuclear Oligomeric Muscle LIM...
Prolonged hemodynamic overload results in cardiac hypertrophy and failure with detrimental changes in myocardial gene expression and morphology. It has been suggested that CSRP3 or muscle LIM protein (MLP) is a mechano-sensor in cardiac myocytes, relaying messages from the myofilaments to the nucleus. Therefore, the subcellular location of MLP may have important functional implications in health and disease. Our hypothesis is that MLP becomes mislocalized after prolonged overload resulting in impaired mechanosensing in cardiac myocytes. Using the techniques of biochemical subcellular fractionation and immunocytochemistry, we found MLP exhibits oligomerization in the membrane and cytoskeleton of cultured cardiac rat neonatal myocytes. However, nuclear MLP was always monomeric. MLP translocated to the nucleus and nucleolus in response to 10% cyclic stretch at 1Hz for 48 hours. This translocation was associated with a 3 fold increase in S6 ribosomal protein (p,0.01 n=3 cultures). Adenoviral ...
http://circ.ahajournals.org/content/114/Suppl_18/II_138.2
*  Mutations in the Human Muscle LIM Protein Gene in Families With Hypertrophic Cardiomyopathy | Circulation
In family B, 3 individuals were found to have the Ser54Arg/Glu55Gly mutations (II:2, II:3, and II:4). Individual II:2 reported exertional dyspnea and palpitations at the age of 44 years. He had marked concentric left ventricular hypertrophy with severely impaired diastolic compliance, first-degree AV block, and ST-segment depressions in left anterior ECG leads. Holter ECG revealed paroxysmal atrial fibrillation and ventricular tachycardias (Lown class IVb). Individual II:3 reported exertional dyspnea; echocardiography revealed pathological septal TDI indices in the absence of hypertrophy. Individual II:4 reported palpitations and angina. On ECG, she had left ventricular hypertrophy with repolarization changes and deep S V2/V3 (fulfilling 1 major plus 1 minor ECG criterion of HCM). On echocardiography, she showed regional hypertrophy in the proximal septum; normal indices were recorded on TDI. The father (I:1) had died of sudden death at the age of 77 years. He had reported palpitations and ...
http://circ.ahajournals.org/content/107/10/1390
*  Filamin-binding LIM protein 1
This gene encodes a protein with an N-terminal filamin-binding domain, a central proline-rich domain, and, multiple C-terminal LIM domains. This protein localizes at cell junctions and may link cell adhesion structures to the actin cytoskeleton. This protein may be involved in the assembly and stabilization of actin-filaments and likely plays a role in modulating cell adhesion, cell morphology and cell motility. This protein also localizes to the nucleus and may affect cardiomyocyte differentiation after binding with the CSX/NKX2-5 transcription factor. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008 ...
https://pharos.nih.gov/idg/targets/Q8WUP2
*  Downregulation of Cytoskeletal Muscle LIM Protein by Nitric Oxide. Impact on Cardiac Myocyte Hypertrophy | Circulation
Thank you for your interest in spreading the word on Circulation.. NOTE: We only request your email address so that the person you are recommending the page to knows that you wanted them to see it, and that it is not junk mail. We do not capture any email address. ...
http://circ.ahajournals.org/content/early/2003/03/03/01.CIR.0000055319.94801.FC
*  FBLIM1 Full-Length MS Protein Standard - Creative Proteomics
FBLIM1 Full-Length MS Protein Standard (NP_060026), Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. This gene encodes a protein with an N-terminal filamin-binding domain, a central proline-rich domain, and, multiple C-terminal LIM domains. This protein localizes at cell junctions and may link cell adhesion structures to the actin cytoskeleton. This protein may be involved in the assembly and stabilization of actin-filaments and likely plays a role in modulating cell adhesion, cell morphology and cell motility. This protein also localizes to the nucleus and may affect cardiomyocyte differentiation after binding with the CSX/NKX2-5 transcription factor. Alternative splicing results in multiple transcript variants encoding different isoforms.
https://www.creative-proteomics.com/product/detail-cpfl305764_2617.htm
*  Produktübersicht anti-LIM Domain Binding 1 Protein Antikörper
Monoklonale und polyklonale LIM Domain Binding 1 Protein Antikörper für viele Methoden. Ausgesuchte Qualitäts-Hersteller für LIM Domain Binding 1 Protein Antikörper. Hier bestellen.
http://www.antikoerper-online.de/stem-cell-maintenance-pathway-61/lim-domain-binding-1-protein-antibody-26409/
*  LMO1 Gene - GeneCards | RBTN1 Protein | RBTN1 Antibody
Complete information for LMO1 gene (Protein Coding), LIM Domain Only 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
http://www.genecards.org/cgi-bin/carddisp.pl?id_type=entrezgene&id=4004
*  PDZ and LIM domain protein 4
The levels of the EDNRB, HJURP and p60/CAF-1 proteins were strongly associated with overall survival in high-grade gliomas patients (p,0.001, p,0.001 and p=0.002, respectively), whereas the one of PDLI4 was not (P=0.11 ...
https://pharos.nih.gov/idg/targets/P50479
*  anti-LMO2 antibody [4D8] | GeneTex
LMO2 antibody [4D8] (LIM domain only 2) for ELISA, FACS, WB. Anti-LMO2 mAb (GTX60651) is tested in Human samples. 100% Ab-Assurance.
http://www.genetex.com/LMO2-antibody-4D8-GTX60651.html