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Phosphorylation and Reorganization of Keratin Networks: Implications for Carcinogenesis and Epithelial Mesenchymal Transition.

Kim HJ, Choi WJ, Lee CH - Biomol Ther (Seoul) (2015)

Bottom Line: Several endogenous compounds or toxic compounds induce phosphorylation and reorganization of keratin network in cancer cells, leading to increased migration.Continuous phosphorylation of keratin results in loss of keratin, which is one of the features of epithelial mesenchymal transition (EMT).Therefore, several proteins involved in phosphorylation and reorganization of keratin also have a role in EMT.

View Article: PubMed Central - PubMed

Affiliation: BK21PLUS R-FIND team, College of Pharmacy, Dongguk University, Seoul 100-715, Republic of Korea.

ABSTRACT
Metastasis is one of hallmarks of cancer and a major cause of cancer death. Combatting metastasis is highly challenging. To overcome these difficulties, researchers have focused on physical properties of metastatic cancer cells. Metastatic cancer cells from patients are softer than benign cancer or normal cells. Changes of viscoelasticity of cancer cells are related to the keratin network. Unexpectedly, keratin network is dynamic and regulation of keratin network is important to the metastasis of cancer. Keratin is composed of heteropolymer of type I and II. Keratin connects from the plasma membrane to nucleus. Several proteins including kinases, and protein phosphatases bind to keratin intermediate filaments. Several endogenous compounds or toxic compounds induce phosphorylation and reorganization of keratin network in cancer cells, leading to increased migration. Continuous phosphorylation of keratin results in loss of keratin, which is one of the features of epithelial mesenchymal transition (EMT). Therefore, several proteins involved in phosphorylation and reorganization of keratin also have a role in EMT. It is likely that compounds controlling phosphorylation and reorganization of keratin are potential candidates for combating EMT and metastasis.

No MeSH data available.


Related in: MedlinePlus

Keratin in epithelial cells. Desmosome junction: Desmosomes link to the keratin filament of cells. Transmembrane desmosomal cadherins, desmoglein and desmocolin, bind placoglobin, the armadillo family protein, which holds the plectin, plakin family member (Fuchs and Raghavan, 2002). The cytoplasmic plaque anchors the keratin intermediate to the desmosome. Hemidesmosome junction: Integrin α and β heterodimers consist of the core of the hemidesmosome, along with BPAG2, a transmembrane protein. BPAG1e and plectin are two hemidesmosomal proteins that are members of the plakin family (Haines and Lane, 2012). They seem to function by connecting the keratin filament to the transmembrane proteins in the hemidesmosome. BPAG1e, bullous pemphigoid antigen 1, epidermal isoform; BPAG2, bullous pemphigoid antigen 2 (Haines and Lane, 2012). Nuclear junction: Nesprin 3 attach to SUN proteins through the perinucelar space and can directly connect to keratin proteins via plectin (Gerlitz and Bustin, 2011). Modified and combined from Fuchs and Raghavan, Gerlitz and Bustin, and Haines and Lanel (Fuchs and Raghavan, 2002; Gerlitz and Bustin, 2011; Haines and Lane, 2012).
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f4-bt-23-301: Keratin in epithelial cells. Desmosome junction: Desmosomes link to the keratin filament of cells. Transmembrane desmosomal cadherins, desmoglein and desmocolin, bind placoglobin, the armadillo family protein, which holds the plectin, plakin family member (Fuchs and Raghavan, 2002). The cytoplasmic plaque anchors the keratin intermediate to the desmosome. Hemidesmosome junction: Integrin α and β heterodimers consist of the core of the hemidesmosome, along with BPAG2, a transmembrane protein. BPAG1e and plectin are two hemidesmosomal proteins that are members of the plakin family (Haines and Lane, 2012). They seem to function by connecting the keratin filament to the transmembrane proteins in the hemidesmosome. BPAG1e, bullous pemphigoid antigen 1, epidermal isoform; BPAG2, bullous pemphigoid antigen 2 (Haines and Lane, 2012). Nuclear junction: Nesprin 3 attach to SUN proteins through the perinucelar space and can directly connect to keratin proteins via plectin (Gerlitz and Bustin, 2011). Modified and combined from Fuchs and Raghavan, Gerlitz and Bustin, and Haines and Lanel (Fuchs and Raghavan, 2002; Gerlitz and Bustin, 2011; Haines and Lane, 2012).

Mentions: In the epithelia tissues, a network of proteins links the nucleus to membrane of cell through keratin filaments, in which transmembrane proteins gives the ground for cell to cell and cell to extracellular matrix adhesion (Fig. 4) (Omary et al., 2009; Pan et al., 2013).


Phosphorylation and Reorganization of Keratin Networks: Implications for Carcinogenesis and Epithelial Mesenchymal Transition.

Kim HJ, Choi WJ, Lee CH - Biomol Ther (Seoul) (2015)

Keratin in epithelial cells. Desmosome junction: Desmosomes link to the keratin filament of cells. Transmembrane desmosomal cadherins, desmoglein and desmocolin, bind placoglobin, the armadillo family protein, which holds the plectin, plakin family member (Fuchs and Raghavan, 2002). The cytoplasmic plaque anchors the keratin intermediate to the desmosome. Hemidesmosome junction: Integrin α and β heterodimers consist of the core of the hemidesmosome, along with BPAG2, a transmembrane protein. BPAG1e and plectin are two hemidesmosomal proteins that are members of the plakin family (Haines and Lane, 2012). They seem to function by connecting the keratin filament to the transmembrane proteins in the hemidesmosome. BPAG1e, bullous pemphigoid antigen 1, epidermal isoform; BPAG2, bullous pemphigoid antigen 2 (Haines and Lane, 2012). Nuclear junction: Nesprin 3 attach to SUN proteins through the perinucelar space and can directly connect to keratin proteins via plectin (Gerlitz and Bustin, 2011). Modified and combined from Fuchs and Raghavan, Gerlitz and Bustin, and Haines and Lanel (Fuchs and Raghavan, 2002; Gerlitz and Bustin, 2011; Haines and Lane, 2012).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4489823&req=5

f4-bt-23-301: Keratin in epithelial cells. Desmosome junction: Desmosomes link to the keratin filament of cells. Transmembrane desmosomal cadherins, desmoglein and desmocolin, bind placoglobin, the armadillo family protein, which holds the plectin, plakin family member (Fuchs and Raghavan, 2002). The cytoplasmic plaque anchors the keratin intermediate to the desmosome. Hemidesmosome junction: Integrin α and β heterodimers consist of the core of the hemidesmosome, along with BPAG2, a transmembrane protein. BPAG1e and plectin are two hemidesmosomal proteins that are members of the plakin family (Haines and Lane, 2012). They seem to function by connecting the keratin filament to the transmembrane proteins in the hemidesmosome. BPAG1e, bullous pemphigoid antigen 1, epidermal isoform; BPAG2, bullous pemphigoid antigen 2 (Haines and Lane, 2012). Nuclear junction: Nesprin 3 attach to SUN proteins through the perinucelar space and can directly connect to keratin proteins via plectin (Gerlitz and Bustin, 2011). Modified and combined from Fuchs and Raghavan, Gerlitz and Bustin, and Haines and Lanel (Fuchs and Raghavan, 2002; Gerlitz and Bustin, 2011; Haines and Lane, 2012).
Mentions: In the epithelia tissues, a network of proteins links the nucleus to membrane of cell through keratin filaments, in which transmembrane proteins gives the ground for cell to cell and cell to extracellular matrix adhesion (Fig. 4) (Omary et al., 2009; Pan et al., 2013).

Bottom Line: Several endogenous compounds or toxic compounds induce phosphorylation and reorganization of keratin network in cancer cells, leading to increased migration.Continuous phosphorylation of keratin results in loss of keratin, which is one of the features of epithelial mesenchymal transition (EMT).Therefore, several proteins involved in phosphorylation and reorganization of keratin also have a role in EMT.

View Article: PubMed Central - PubMed

Affiliation: BK21PLUS R-FIND team, College of Pharmacy, Dongguk University, Seoul 100-715, Republic of Korea.

ABSTRACT
Metastasis is one of hallmarks of cancer and a major cause of cancer death. Combatting metastasis is highly challenging. To overcome these difficulties, researchers have focused on physical properties of metastatic cancer cells. Metastatic cancer cells from patients are softer than benign cancer or normal cells. Changes of viscoelasticity of cancer cells are related to the keratin network. Unexpectedly, keratin network is dynamic and regulation of keratin network is important to the metastasis of cancer. Keratin is composed of heteropolymer of type I and II. Keratin connects from the plasma membrane to nucleus. Several proteins including kinases, and protein phosphatases bind to keratin intermediate filaments. Several endogenous compounds or toxic compounds induce phosphorylation and reorganization of keratin network in cancer cells, leading to increased migration. Continuous phosphorylation of keratin results in loss of keratin, which is one of the features of epithelial mesenchymal transition (EMT). Therefore, several proteins involved in phosphorylation and reorganization of keratin also have a role in EMT. It is likely that compounds controlling phosphorylation and reorganization of keratin are potential candidates for combating EMT and metastasis.

No MeSH data available.


Related in: MedlinePlus