scholarly journals DNA damage-dependent interaction of the nuclear matrix protein C1D with translin-associated factor X (TRAX)

2002 ◽  
Vol 115 (1) ◽  
pp. 207-216 ◽  
Author(s):  
Tuba Erdemir ◽  
Bilada Bilican ◽  
Dilhan Oncel ◽  
Colin R. Goding ◽  
Ugur Yavuzer
Keyword(s):  
Nuclear Matrix ◽  
Mammalian Cells ◽  
Matrix Protein ◽  
Biological Function ◽  
Factor X ◽  
Nuclear Targeting ◽  
Γ Irradiation ◽  
Nuclear Matrix Protein ◽  
Associated Factor

The nuclear matrix protein C1D is an activator of the DNA-dependent protein kinase (DNA-PK), which is essential for the repair of DNA double-strand breaks (DSBs) and V(D)J recombination. C1D is phosphorylated very efficiently by DNA-PK, and its mRNA and protein levels are induced upon γ-irradiation, suggesting that C1D may play a role in repair of DSBs in vivo. In an attempt to identify the biological function of C1D, we have employed the yeast two-hybrid system and found that C1D interacts specifically with Translin-associated factor X, TRAX. Although the biological function of TRAX remains unknown, its bipartite nuclear targeting sequences suggest a role for TRAX in the movement of associated proteins, including Translin, into the nucleus. We show that C1D and TRAX interact specifically in both yeast and mammalian cells. Interestingly, however, interaction of these two proteins in mammalian cells only occur following γ-irradiation, raising the possibility of involvement of TRAX in DNA double-strand break repair and providing evidence for biological functions of the nuclear matrix protein C1D and TRAX. Moreover, we show, using fluorescently tagged proteins, that the relative expression levels of TRAX and Translin affect their subcellular localization. These results suggest that one role for C1D may be to regulate TRAX/Translin complex formation.

scholarly journals Phosphorylation-related accumulation of the 125K nuclear matrix protein mitotin in human mitotic cells

1990 ◽  
Vol 95 (1) ◽  
pp. 59-64
Author(s):  
N.Z. Zhelev ◽  
I.T. Todorov ◽  
R.N. Philipova ◽  
A.A. Hadjiolov
Keyword(s):  
Nuclear Matrix ◽  
Mammalian Cells ◽  
Matrix Protein ◽  
Specific Protein ◽  
S Phase ◽  
Short Term ◽  
Nuclear Matrix Protein ◽  
Complex Events ◽  
G2 Phase ◽  
Mitotic Cells

The preparation of mammalian cells for entry into mitosis is related to a cascade of G2 phase phosphorylations of several nuclear proteins driven by mitosis-specific protein kinases. Using a monoclonal antibody we have identified previously in mammalian cells a 125K/pI6.5 protein, associated with the nuclear matrix, and markedly increased in mitotic cells, which was named ‘mitotin’. Here, we show by short-term [35S]methionine labeling of cell cycle synchronized cells that this protein is synthesized at comparable rates throughout interphase. However, upon cycloheximide block of protein synthesis mitotin labeled during S phase is rapidly degraded, while the degradation of mitotin labeled during late G2 phase is abolished, resulting in its net and marked increase. The accumulation of mitotin in premitotic and mitotic cells is related to its phosphorylation and the metabolic stability of its two phosphorylated forms. The metabolic stabilization and accumulation of a nuclear matrix protein upon phosphorylation suggests the operation of a novel mechanism among the complex events preparing the cell for mitosis.

scholarly journals The amino-terminal region of the retinoblastoma gene product binds a novel nuclear matrix protein that co-localizes to centers for RNA processing.

1994 ◽  
Vol 127 (3) ◽  
pp. 609-622 ◽  
Author(s):  
T Durfee ◽  
M A Mancini ◽  
D Jones ◽  
S J Elledge ◽  
W H Lee
Keyword(s):  
Nuclear Matrix ◽  
Rna Processing ◽  
Matrix Protein ◽  
Terminal Region ◽  
Cellular Proteins ◽  
Amino Terminus ◽  
Nuclear Matrix Protein ◽  
Amino Terminal

The tumor suppressing capacity of the retinoblastoma protein (p110RB) is dependent on interactions made with cellular proteins through its carboxy-terminal domains. How the p110RB amino-terminal region contributes to this activity is unclear, though evidence now indicates it is important for both growth suppression and regulation of the full-length protein. We have used the yeast two-hybrid system to screen for cellular proteins which bind to the first 300 amino acids of p110RB. The only gene isolated from this screen encodes a novel 84-kD nuclear matrix protein that localizes to subnuclear regions associated with RNA processing. This protein, p84, requires a structurally defined domain in the amino terminus of p110RB for binding. Furthermore, both in vivo and in vitro experiments demonstrate that p84 binds preferentially to the functionally active, hypophosphorylated form of p110RB. Thus, the amino terminus of p110RB may function in part to facilitate the binding of growth promoting factors at subnuclear regions actively involved in RNA metabolism.

scholarly journals An episomally replicating vector binds to the nuclear matrix protein SAF‐A in vivo

EMBO Reports ◽  
2002 ◽  
Vol 3 (4) ◽  
pp. 349-354 ◽  
Author(s):  
Bok Hee C Jenke ◽  
Christian P Fetzer ◽  
Isa M Stehle ◽  
Franziska Jönsson ◽  
Frank O Fackelmayer ◽  
...  
Keyword(s):  
Nuclear Matrix ◽  
Matrix Protein ◽  
Nuclear Matrix Protein

Induction of apoptosis in breast cancer cells in response to vitamin D and antiestrogens

1994 ◽  
Vol 72 (11-12) ◽  
pp. 537-545 ◽  
Author(s):  
JoEllen Welsh
Keyword(s):  
Breast Cancer ◽  
Vitamin D ◽  
Nuclear Matrix ◽  
Matrix Protein ◽  
Combined Treatment ◽  
Cell Number ◽  
Nuclear Matrix Protein ◽  
Mcf 7

1,25-Dihydroxycholecalciferol D3 (1,25(OH)2D3), the active metabolite of vitamin D, is a potent inhibitor of breast cancer cell growth both in vivo and in vitro. We have shown that MCF-7 cells treated with 100 nM 1,25(OH)2D3 exhibit characteristic apoptotic morphology (pyknotic nuclei, chromatin and cytoplasmic condensation, nuclear matrix protein reorganization) within 48 h. In the experiments reported here, we examined the interactions between 1,25(OH)2D3 and the antiestrogen 4-hydroxytamoxifen (TAM), which also induces apoptosis in MCF-7 cells. Our data suggest that TAM significantly potentiates the reduction in cell number induced by 1,25(OH)2D3 alone. Combined treatment with 1,25(OH)2D3 and TAM enhances the degree of apoptosis assessed using morphological markers that identify chromatin and nuclear matrix protein condensation. We have selected a subclone of MCF-7 cells resistant to 1,25(OH)2D3 (MCF-7D3Res). These cells express the vitamin D receptor and exhibit doubling times comparable to the parental MCF-7 cells, even when grown in 100 mM 1,25(OH)2D3. Treatment of both parental and resistant MCF-7 cells with TAM induces apoptosis and clusterin. These data emphasize that apoptosis can be induced in MCF-7 cells either by activation of vitamin-D-mediated signalling or disruption of estrogen-dependent signalling.Key words: apoptosis, breast, vitamin D, antiestrogen, gene expression, clusterin.

scholarly journals The β4 Integrin Interactor p27BBP/eIF6 Is an Essential Nuclear Matrix Protein Involved in 60S Ribosomal Subunit Assembly

1999 ◽  
Vol 144 (5) ◽  
pp. 823-838 ◽  
Author(s):  
Francesca Sanvito ◽  
Simonetta Piatti ◽  
Antonello Villa ◽  
Mario Bossi ◽  
Giovanna Lucchini ◽  
...  
Keyword(s):  
Nuclear Matrix ◽  
Mammalian Cells ◽  
Matrix Protein ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Integrin Subunit ◽  
Topographical Distribution ◽  
Evolutionarily Conserved ◽  
Β4 Integrin

p27BBP/eIF6 is an evolutionarily conserved protein that was originally identified as p27BBP, an interactor of the cytoplasmic domain of integrin β4 and, independently, as the putative translation initiation factor eIF6. To establish the in vivo function of p27BBP/eIF6, its topographical distribution was investigated in mammalian cells and the effects of disrupting the corresponding gene was studied in the budding yeast, Saccharomyces cerevisiae. In epithelial cells containing β4 integrin, p27BBP/eIF6 is present in the cytoplasm and enriched at hemidesmosomes with a pattern similar to that of β4 integrin. Surprisingly, in the absence and in the presence of the β4 integrin subunit, p27BBP/eIF6 is in the nucleolus and associated with the nuclear matrix. Deletion of the IIH S. cerevisiae gene, encoding the yeast p27BBP/eIF6 homologue, is lethal, and depletion of the corresponding gene product is associated with a dramatic decrease of the level of free ribosomal 60S subunit. Furthermore, human p27BBP/eIF6 can rescue the lethal effect of the iihΔ yeast mutation. The data obtained in vivo suggest an evolutionarily conserved function of p27BBP/eIF6 in ribosome biogenesis or assembly rather than in translation. A further function related to the β4 integrin subunit may have evolved specifically in higher eukaryotic cells.

984: Variability in the Performance of Nuclear Matrix Protein 22 in the Detection of Bladder Cancer

2006 ◽  
Vol 175 (4S) ◽  
pp. 317-317
Author(s):  
Shahrokh F. Shariat ◽  
Michael Marberger ◽  
Yair Lotan ◽  
Marta Sanchez-Carbayo ◽  
Craig D. Zippe ◽  
...  
Keyword(s):  
Bladder Cancer ◽  
Nuclear Matrix ◽  
Matrix Protein ◽  
Nuclear Matrix Protein

Sa1664 Identification of Nuclear Matrix Protein Alternations Associated With Autophagic Dysfunction in the Liver

2016 ◽  
Vol 150 (4) ◽  
pp. S1090
Author(s):  
Shunhei Yamashina ◽  
Kousuke Izumi ◽  
Yoshihiro Inami ◽  
Tomonori Aoyama ◽  
Akira Uchiyama ◽  
...  
Keyword(s):  
Nuclear Matrix ◽  
Matrix Protein ◽  
Nuclear Matrix Protein
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