Islet expression of Rhombotin and Isl-1 suggests cell type specific exposure of LIM-domain epitopes

Lund, Kaare; Petersen, Jacob Sten; Jensen, Jan; Blume, Niels; Edlund, Thomas; Thor, Stefan; Madsen, Ole

doi:10.1007/bf02935644

Cited by 4 publications

(5 citation statements)

References 43 publications

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“…Therefore, this study paid special attention to these three genes. We found that the protein products of the ISL-1 gene are similar to those of the MEC-3 (31) and LIN-11 (32,33) genes in that they have a cysteine-rich pattern upstream of the homologous domain. (34,35), because zinc finger proteins bind to DNA and regulate gene activity.…”

Section: Discussionmentioning

confidence: 75%

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Effect of LHX2 gene methylation level and its function on radiotherapy of cervical cancer

Yu¹,

Zhang²,

Yu³

et al. 2021

Transl Cancer Res TCR

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Background: Cervical cancer is the most common malignancy of the female reproductive system, for which radiotherapy is one of the main treatments. Gene methylation in cells is an important factor in tumorigenesis, and radiotherapy can change DNA methylation in cells. At the same time, combined with the clinical effect of radiotherapy, key genes of LIM homeobox 2 (LHX2) significantly related to cervical cancer.The LHX2 are LIM-homeobox genes that play important roles in signal transduction, cell differentiation, tissue-specific differentiation, and body formation.Methods: In this study, bisulfite genomic sequencing (BSP-Seq) technology was used to analyze the methylation level of LHX2 in patients with cervical cancer before and after radiotherapy. In addition, combined with the clinical effect of radiotherapy, the function of LHX2 in siHA and C33A cells were analyzed with the help of overexpression, small interfering RNA (siRNA), cell invasion, and migration ability.The expression level of the migration-and apoptosis-related genes which were affected by LHX2 were tested with quantitative real time polymerase chain reaction (qRT-PCR).Results: Combined with clinical treatment, methylation level difference, and correlation enrichment analysis, it was found that LHX2 genes were closely related to the occurrence and development of cervical cancer. After 5-aza-2'-deoxycytidine (5-Aza-dC) and radiotherapy, the methylation of LHX2 genes in siHA and C33A squamous cell carcinoma cells was decreased, and the messenger RNA (mRNA) and protein expression levels were relatively increased; meanwhile, the LHX2 could accelerate the ability for cell invasion and migration and inhibited the apoptosis of the cell after treatment with radiotherapy. Conclusions:The methylation and expression levels of LHX2 genes are closely related to cervical cancer.The methylation level of LHX2 was reduced after radiation therapy. The LHX2 gene has a positive effect on cervical cancer through acceleration of the cell invasion and migration ability and inhibition of cell apoptosis after radiotherapy treatment.

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Section: Discussionmentioning

confidence: 75%

“…We found that the protein products of the ISL - 1 gene are similar to those of the MEC - 3 ( 31 ) and LIN - 11 ( 32 , 33 ) genes in that they have a cysteine-rich pattern upstream of the homologous domain. Therefore, the pattern containing similar structures is called LIM.…”

Section: Discussionmentioning

confidence: 80%

Effect of LHX2 gene methylation level and its function on radiotherapy of cervical cancer

Yu¹,

Zhang²,

Yu³

et al. 2021

Transl Cancer Res TCR

View full text Add to dashboard Cite

show abstract

“…All experiments were performed in duplicate with at least three independent experiments executed and tabulated to determine mean and SD from the mean. Statistical analyses were performed with Student's t test; *, p Ͻ 0.05; **, p Ͻ 0.01. main proteins Isl-1 and LMO-1 (Lund et al, 1995) although the mechanism is unknown.…”

Section: Discussionmentioning

confidence: 99%

Serine and Threonine Phosphorylation of the Paxillin LIM Domains Regulates Paxillin Focal Adhesion Localization and Cell Adhesion to Fibronectin

Brown

Perrotta

Turner

1998

MBoC

128

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We have previously shown that the LIM domains of paxillin operate as the focal adhesion (FA)-targeting motif of this protein. In the current study, we have identified the capacity of paxillin LIM2 and LIM3 to serve as binding sites for, and substrates of serine/ threonine kinases. The activities of the LIM2-and LIM3-associated kinases were stimulated after adhesion of CHO.K1 cells to fibronectin; consequently, a role for LIM domain phosphorylation in regulating the subcellular localization of paxillin after adhesion to fibronectin was investigated. An avian paxillin-CHO.K1 model system was used to explore the role of paxillin phosphorylation in paxillin localization to FAs. We found that mutations of paxillin that mimicked LIM domain phosphorylation accelerated fibronectin-induced localization of paxillin to focal contacts. Further, blocking phosphorylation of the LIM domains reduced cell adhesion to fibronectin, whereas constitutive LIM domain phosphorylation significantly increased the capacity of cells to adhere to fibronectin. The potentiation of FA targeting and cell adhesion to fibronectin was specific to LIM domain phosphorylation as mutation of the amino-terminal tyrosine and serine residues of paxillin that are phosphorylated in response to fibronectin adhesion had no effect on the rate of FA localization or cell adhesion. This represents the first demonstration of the regulation of protein localization through LIM domain phosphorylation and suggests a novel mechanism of regulating LIM domain function. Additionally, these results provide the first evidence that paxillin contributes to "inside-out" integrin-mediated signal transduction.

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“…A conformational change associated with phosphorylation of the focal adhesion protein vinculin has also been shown to regulate vinculin actin-binding potential [Weekes et al, 1996;Schwienbacher et al, 1996], and phosphorylation of talin, ␤-catenin, and paxillin have been associated with alteration in subcellular localization [Miller and Moon, 1997;Turner et al, 1989;Brown et al, 1998]. Interestingly, cell activation results in the differential presentation of LIM epitopes of the proteins rhombotin and Isl-1 [Lund et al, 1995]. Thus, paxillin LIM phosphorylation may act as a switch that regulates the conformational interplay between the LIM domains, the activity of the focal adhesion targeting motif, and the multiple protein-protein interaction domains present within this molecule.…”

Section: Discussionmentioning

confidence: 94%

Characterization of paxillin LIM domain-associated serine threonine kinases: Activation by angiotensin II in vascular smooth muscle cells

Brown

Turner

2000

J. Cell. Biochem.

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Recently we reported a novel means of regulating LIM domain protein function. Paxillin LIM zinc-finger phosphorylation in response to cell adhesion regulates the subcellular localization of this cytoskeletal adaptor protein to focal adhesions, and also modulates cell adhesion to fibronectin Mol. Biol. Cell 9:1803-1816). In the present study, we characterize further the protein kinases that phosphorylate paxillin LIM2 on threonine and LIM3 on serine. Analysis of the subcellular distribution of the LIM kinases demonstrated that the LIM3 protein kinase, but not the LIM2 kinase, resides within a detergent-insoluble fraction. The activities of the paxillin LIM domain kinases are differentially regulated during embryogenesis, and analysis of tissue distribution indicated a specificity in expression patterns between the LIM2 and LIM3 kinases. In addition, these protein kinases were refractory to inhibition by a panel of broad-spectrum serine/threonine kinase inhibitors, suggesting a novel derivation. The paxillin protein kinase activities were stimulated in serum-starved CHO.K1 cells by the mitogen phorbol myristate acetate (PMA), and by PMA and angiotensin II in rat aortic smooth muscle cells. In vivo labeling, phosphoamino acid analysis, and phosphopeptide mapping of paxillin immunoprecipitated from angiotensin II-stimulated smooth muscle cells confirmed an induction of paxillin serine/threonine phosphorylation and supports the contention that these newly identified paxillin kinases are dynamic components of growth factor signaling through the cytoskeleton.

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Islet expression of Rhombotin and Isl-1 suggests cell type specific exposure of LIM-domain epitopes

Cited by 4 publications

References 43 publications

Effect of LHX2 gene methylation level and its function on radiotherapy of cervical cancer

Effect of LHX2 gene methylation level and its function on radiotherapy of cervical cancer

Serine and Threonine Phosphorylation of the Paxillin LIM Domains Regulates Paxillin Focal Adhesion Localization and Cell Adhesion to Fibronectin

Characterization of paxillin LIM domain-associated serine threonine kinases: Activation by angiotensin II in vascular smooth muscle cells

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