Plectin deficiency on cytoskeletal disorganization and transformation of human liver cells in vitro

Liu, Yi-Hsiang; Cheng, Chiung-Chi; Ho, Ching-Chun; Chao, Wei‐Ting; Pei, Ren-Jeng; Hsu, Yung-Hsiang; Ho, Lu-Chang; Shiu, Bei-Hao; Lai, Yih-Shyong

doi:10.1007/s00795-010-0499-y

Cited by 18 publications

(14 citation statements)

References 21 publications

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“…FAM83H-FLAG immunoprecipitates contained plectin (supplementary material Table S1), and plectin knockdown, as well as the inhibition of FAM83H and CK-1a, caused keratin filament bundling in HCT116 cells (supplementary material Fig. S3) and a human liver cell line (Liu et al, 2011). Our next task will be proteomic analysis to identify the CK-1a substrates responsible for the rearrangement of keratin filaments.…”

Section: Discussionmentioning

confidence: 99%

“…The plakin family proteins, which are linker proteins between keratin filaments and various cytoskeletal structures (Wiche, 1998), are major modulators of keratin filament bundling (Boczonadi et al, 2007;Liu et al, 2011;Long et al, 2006;Osmanagic-Myers et al, 2006); however, our knowledge about crucial modulators of keratin filament bundling remains very limited. To further understand the mechanism governing the rearrangement of keratin filaments, identification of novel keratin-associated proteins and kinases responsible for the mechanism is required.…”

Section: Introductionmentioning

confidence: 99%

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A novel mechanism of keratin cytoskeleton organization through casein kinase Iα and FAM83H in colorectal cancer

Kuga

Kume

Kawasaki

et al. 2013

Journal of Cell Science

134

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SummaryKeratin filaments form cytoskeletal networks in epithelial cells. Dynamic rearrangement of keratin filament networks is required for epithelial cells to perform cellular processes such as cell migration and polarization; however, the mechanism governing keratin filament rearrangement remains unclear. Here, we describe a novel mechanism of keratin cytoskeleton organization mediated by casein kinase Ia (CK-1a) and a newly identified keratin-associated protein, FAM83H. Knockdown of FAM83H induces keratin filament bundling, whereas overexpression of FAM83H disassembles keratin filaments, suggesting that FAM83H regulates the filamentous state of keratins. Intriguingly, keratin filament bundling is concomitant with the dissociation of CK-1a from keratin filaments, whereas aberrant speckle-like localization of CK-1a is observed concomitantly with keratin filament disassembly. Furthermore, CK-1a inhibition, similar to FAM83H knockdown, causes keratin filament bundling and reverses keratin filament disassembly induced by FAM83H overexpression, suggesting that CK-1a mediates FAM83H-dependent reorganization of keratin filaments. Because the N-terminal region of FAM83H interacts with CK-1a and the C-terminal region interacts with keratins, FAM83H might tether CK-1a to keratins. Colorectal cancer tissue also shows keratin filament disassembly accompanied with FAM83H overexpression and aberrant CK-1a localization, and FAM83H-overexpressing cancer cells exhibit loss or alteration of epithelial cell polarity. Importantly, knockdown of FAM83H inhibits cell migration accompanied by keratin cytoskeleton rearrangement in colorectal cancer cells. These results suggest that keratin cytoskeleton organization is regulated by FAM83H-mediated recruitment of CK-1a to keratins, and that keratin filament disassembly caused by overexpression of FAM83H and aberrant localization of CK-1a could contribute to the progression of colorectal cancer.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A novel mechanism of keratin cytoskeleton organization through casein kinase Iα and FAM83H in colorectal cancer

Kuga

Kume

Kawasaki

et al. 2013

Journal of Cell Science

134

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“…The cross-linking functions of plectin help organize the cytoskeleton into a stable meshwork that is important for maintaining uniformity of cell size and shape. In one study (30), expression of CK18 was shown to be downregulated by suppression of plectin protein, and cytokeratin networks (12,14,(22)(23)(24) and of ERK1/2 in the ERK MAPK pathway (28,29), and regulation of CK18 by Wnt is involved in Akt activation (26,27). Questions regarding the PI3K/Akt and Wnt pathways, and whether CK18 functions as the regulator in these three pathways require further investigation.…”

Section: Interactions With Related Proteinsmentioning

confidence: 99%

Biological Functions of Cytokeratin 18 in Cancer

Weng

Cui²,

Fang³

2012

Molecular Cancer Research

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The structural proteins cytokeratin 18 (CK18) and its coexpressed complementary partner CK8 are expressed in a variety of adult epithelial organs and may play a role in carcinogenesis. In this study, we focused on the biological functions of CK18, which is thought to modulate intracellular signaling and operates in conjunction with various related proteins. CK18 may affect carcinogenesis through several signaling pathways, including the phosphoinositide 3-kinase (PI3K)/Akt, Wnt, and extracellular signal-regulated kinase (ERK) mitogen-activated protein kinase (MAPK) signaling pathways. CK18 acts as an identical target of Akt in the PI3K/Akt pathway and of ERK1/2 in the ERK MAPK pathway, and regulation of CK18 by Wnt is involved in Akt activation. Finally, we discuss the importance of gaining a more complete understanding of the expression of CK18 during carcinogenesis, and suggest potential clinical applications of that understanding. Mol Cancer Res; 10(4); 485-93. Ó2012 AACR.

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“…Therefore, it is assumed that tongue epithelial cells have a "thin" cell structure and that the cytoskeleton is maintained by an intercellular component. Plectin-1 knock down in human liver cells treated with plectin-1 siRNA was shown to induce a decrease in the expression of CK18, the disorganization of intermediate filaments, and an increase in actin fibers [18]. Accordingly, chief cytoskeleton components in human tongue epithelial cells could be other molecules such as actin, tubulin, and heat shock proteins [19].…”

Section: Discussionmentioning

confidence: 99%

Expression of Plectin-1 and Trichohyalin in Human Tongue Cancer Cells

Tamura¹,

Ueda²,

Nishikawa³

et al. 2018

OJST

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In basal squamous cells, plectin-1 interacts with intermediate filaments, whereas trichohyalin, which is distributed primarily in the medulla and inner root sheath cells of human hair follicles, plays a role in strengthening cells during keratinization. Although both cytoskeletal proteins occur in trace amounts in human tongue epithelial cells, there are minimal data on their expression in human tongue primary cancer cells. We therefore investigated the expression of plectin-1 and trichohyalin in human tongue epithelial cell line (DOK) and tongue cancer cell line (BICR31) using western blotting and FITC-labeled immunocytochemistry techniques. DOK and BICR31 cells were cultivated to subconfluence in Dulbecco's Modified Eagle's Medium containing 0.4 µg/ml of hydrocortisone and 10% fetal bovine serum, and the levels of trichohyalin and plectin-1 were determined by western blot analysis and immunocytochemical staining. Trichohyalin expression was clearly observed, with no differences between DOK and BICR31 cells. Although DOK cells expressed trace levels of plectin-1, obvious plectin-1 bands were detected in western blot analyses of BICR31 cells. Immunocytochemical staining revealed that trichohyalin and plectin-1 localize in the cytoplasm. Trichohyalin was diffusely distributed in both cell lines, and colocalization of trichohyalin and cytokeratin 1/10 was observed in almost all BICR31 cells. There were no correlations between western blot and immunocytochemical data for trichohyalin. Conversely, correlations in immunochemical reactions for plectin-1 were observed. Most DOK cells showed no localization of plectin-1, but strong reactions were detected in the cytoplasm of BICR31 cells. These results indicate that trichohyalin is expressed by cancerous tongue epithelial cells during various stages of malignancy and that plectin-1 provides an index of malignancy.

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Plectin deficiency on cytoskeletal disorganization and transformation of human liver cells in vitro

Cited by 18 publications

References 21 publications

A novel mechanism of keratin cytoskeleton organization through casein kinase Iα and FAM83H in colorectal cancer

A novel mechanism of keratin cytoskeleton organization through casein kinase Iα and FAM83H in colorectal cancer

Biological Functions of Cytokeratin 18 in Cancer

Expression of Plectin-1 and Trichohyalin in Human Tongue Cancer Cells

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