A repeating amino acid motif shared by proteins with diverse cellular roles

Peifer, Mark; Berg, Sven; Reynolds, Albert B.

doi:10.1016/0092-8674(94)90353-0

Cited by 625 publications

(438 citation statements)

References 14 publications

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“…The peptide shows 43% sequence homology to other APC arm repeats and at least 37% homology to repeats of further known arm proteins [2]. Thus, the presented results may be considered as a first step towards the structural analysis of other proteins containing the arm motif.…”

Section: Discussionmentioning

confidence: 66%

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Secondary structure of an armadillo single repeat from the APC protein

Hirschl¹,

Bayer²,

Müller³

1996

FEBS Letters

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Section: Discussionmentioning

confidence: 66%

“…Arm motifs were also found in several m~related proteins of different species (for review see [2,3]). All krown arm proteins contain seven to twelve copies of repeats aranged in tandem with very short or no intervening seqt~ences.…”

Section: Introductionmentioning

confidence: 99%

Secondary structure of an armadillo single repeat from the APC protein

Hirschl¹,

Bayer²,

Müller³

1996

FEBS Letters

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“…The ALEX gene family consists of at least three variants (ALEX1, ALEX2, and ALEX3), which have one or two ARM repeat domains. Though the classical ARM family was involved in a variety of processes such as cell adhesion, embryogenesis and tumorigenesis (Peifer et al, 1994;Hatzfeld, 1999), little is known about the ALEX genes. Recent report demonstrates that the ALEX3 directly interacts with the sex determining region Y (Sry)-box 10 (SOX10) transcription factor via the ARM repeat domains and alters its subcellular localization and transcriptional activity (Mou et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

ALEX1 Regulates Proliferation and Apoptosis in Breast Cancer Cells

Gao

Wu²,

Zeng³

et al. 2015

Asian Pacific Journal of Cancer Prevention

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Background: Arm protein lost in epithelial cancers, on chromosome X (ALEX) is a novel subgroup within the armadillo (ARM) family, which has one or two ARM repeat domains as opposed to more than six-thirteen repeats in the classical Armadillo family members. Materials and Methods: In the study, we explore the biological functions of ALEX1 in breast cancer cells. Overexpression of ALEX1 and silencing of ALEX1 were performed with SK-BR3 and MCF-7 cell lines. Cell proliferation and colony formation assays, along with flow cytometry, were carried out to evaluate the roles of ALEX1. Results: ALEX1 overexpression in SK-BR3 breast cancer cells inhibited proliferation and induced apoptosis. Furthermore, depletion of ALEX1 in MCF-7 breast cancer cells increased proliferation and inhibited apoptosis. Additional analyses demonstrated that the overexpression of ALEX1 activated the intrinsic apoptosis cascades through up-regulating the expression of Bax, cytosol cytochrome c, active caspase-9 and active caspase-3 and down-regulating the levels of Bcl-2 and mitochondria cytochrome c. Simultaneouly, silencing of ALEX1 inhibited intrinsic apoptosis cascades through down-regulating the expression of Bax, cytosol cytochrome c, active caspase-9, and active caspase-3 and up-regulating the level of Bcl-2 and mitochondria cytochrome c. Conclusions: Our data suggest that ALEX1 as a crucial tumor suppressor gene has been involved in cell proliferation and apoptosis in breast cancer, which may serve as a novel candidate therapeutic target.

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“…After densitometric evaluation of the arrays, the cell-cell adhesion molecule p120catenin (p120CTN) was found to be upregulated after downregulation of LPXN expression (data not shown). The p120CTN protein is part of a multiprotein cell-cell adhesion complex (Peifer et al, 1994;Reynolds et al, 1994), and its expression is downregulated in approximately 50% of human prostate adenocarcinomas (Kallakury et al, 2001a, b). Quantitative real-time-PCR and western blot analyses clearly confirmed increased p120CTN expression in LPXN small interfering RNAs (siRNA)-transfected cells as compared with luciferase siRNA-transfected control cells (Figure 4a,b).…”

Section: Generation Of Transgenic Mice Expressing Lpxn In Prostate Epmentioning

confidence: 99%

Leupaxin acts as a mediator in prostate carcinoma progression through deregulation of p120catenin expression

et al. 2009

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Recently, we could show that the focal adhesion protein leupaxin (LPXN) is expressed in human prostate carcinomas (PCa) and induces invasiveness of androgenindependent PCa cells. In this study we show that LPXN enhanced the progression of existing PCa in vivo by breeding transgenic mice with prostate-specific LPXN expression and TRAMP mice (transgenic adenocarcinoma of mouse prostate). Double transgenic LPXN/ TRAMP mice showed a significant increase in poorly differentiated PCa and distant metastases as compared with control TRAMP mice. Additional studies on primary PCa cells generated from both transgenic backgrounds confirmed the connection regarding LPXN overexpression and increased motility and invasiveness of PCa cells. One mediator of LPXN-induced invasion was found to be the cell-cell adhesion protein p120catenin (p120CTN). Both in vitro and in vivo experiments revealed that p120CTN expression negatively correlates with LPXN expression, followed by a redistribution of b-catenin. Downregulation of LPXN using small interfering RNAs (siRNAs) resulted in a membranous localization of b-catenin, whereas strong nuclear accumulation of b-catenin was observed in p120CTN knockdown cells leading to enhanced transcription of the b-catenin target gene matrix metalloprotease-7. In conclusion, the present results indicate that LPXN enhances the progression of PCa through downregulation of p120CTN expression and that LPXN could function as a marker for aggressive PCa in the future.

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A repeating amino acid motif shared by proteins with diverse cellular roles

Cited by 625 publications

References 14 publications

Secondary structure of an armadillo single repeat from the APC protein

Secondary structure of an armadillo single repeat from the APC protein

ALEX1 Regulates Proliferation and Apoptosis in Breast Cancer Cells

Leupaxin acts as a mediator in prostate carcinoma progression through deregulation of p120catenin expression

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