Survival-promoting functions of 14-3-3 proteins

2002 ◽  
Vol 30 (4) ◽  
pp. 360-365 ◽  
Author(s):  
S. C. Masters ◽  
R. R. Subramanian ◽  
A. Truong ◽  
H. Yang ◽  
K. Fujii ◽  
...  
Keyword(s):  
Cell Survival ◽  
Anticancer Agents ◽  
Cellular Proteins ◽  
Support Cell ◽  
Antagonist Peptides ◽  
Ligand Interactions ◽  
Cellular Machinery ◽  
In Cells

The 14-3-3 proteins are a family of phosphoserine/phosphothreonine-binding molecules that control the function of a wide array of cellular proteins. We suggest that one function of 14-3-3 is to support cell survival. 14-3-3 proteins promote survival in part by antagonizing the activity of associated proapoptotic proteins, including Bad and apoptosis signal-regulating kinase 1 (ASK1). Indeed, expression of 14-3-3 inhibitor peptides in cells is sufficient to induce apoptosis. Interestingly, these 14-3-3 antagonist peptides can sensitize cells for effective killing by anticancer agents such as cisplatin. Thus, 14-3-3 may be part of the cellular machinery that maintains cell survival, and targeting 14-3-3-ligand interactions may be a useful strategy to enhance the efficacy of conventional anticancer agents.

scholarly journals Hepatitis C virus NS 5A drives a PTEN ‐ PI 3K/Akt feedback loop to support cell survival

2014 ◽  
Vol 35 (6) ◽  
pp. 1682-1691 ◽  
Author(s):  
Du Cheng ◽  
Leiliang Zhang ◽  
Guangbo Yang ◽  
Lei Zhao ◽  
Feng Peng ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Cell Survival ◽  
Feedback Loop ◽  
Support Cell

scholarly journals NF-Y-dependent regulation of glutamate receptor 4 expression and cell survival in cells of the oligodendrocyte lineage

Glia ◽  
2018 ◽  
Vol 66 (9) ◽  
pp. 1896-1914 ◽  
Author(s):  
Ghazala Begum ◽  
Masahiro Otsu ◽  
Usman Ahmed ◽  
Zubair Ahmed ◽  
Adam Stevens ◽  
...  
Keyword(s):  
Cell Survival ◽  
Glutamate Receptor ◽  
In Cells

Specific effect of oestrone sulphate on protein synthesis and secretion by cultured epithelial cells from guinea-pig endometrium

1989 ◽  
Vol 123 (2) ◽  
pp. 233-NP ◽  
Author(s):  
G. Chaminadas ◽  
M. Alkhalaf ◽  
J. P. Rémy-Martin ◽  
A. Y. Propper ◽  
G. L. Adessi
Keyword(s):  
Protein Synthesis ◽  
Epithelial Cells ◽  
Progesterone Receptor ◽  
Guinea Pig ◽  
Cultured Cells ◽  
Polyacrylamide Gel Electrophoresis ◽  
Specific Effect ◽  
Cellular Proteins ◽  
Oestrone Sulphate ◽  
In Cells

ABSTRACT Patterns of induced protein synthesis and secretion in guinea-pig endometrial epithelial cell cultures in response to oestrone sulphate alone and oestrone sulphate plus progesterone were investigated. Epithelial cells were cultured for 3 days in growth medium, then washed three times in a steroid-free medium. For each experiment, anticytokeratin immunostaining was used to discriminate the epithelial cells from the stromal cells. Only experiments in which the control dishes displayed more than 80% of anticytokeratinimmunostained cells were further processed. After this period oestradiol-17β (20 nmol/l; control), oestradiol-17β (20 nmol/l) plus progesterone (0·5 μmol/l), oestrone sulphate (1 μmol/l) or oestrone sulphate (1 μmol/l) plus progesterone (0·5 μmol/l) were added to the medium for 48 h. An immunocytochemical progesterone receptor assay showed that oestradiol-17β increased the progesterone receptor content of cells, and progesterone added to cultured cells in the presence of oestradiol-17β induced a significant increase in oestrogen sulphotransferase activity assessing the hormone responsiveness of the cultured cells. In these culture conditions and after 16 h of incubation, oestradiol-17β induced a 1·7-fold increase in [3H]thymidine incorporation into DNA, and [35S]methionine incorporation into cellular proteins was linearly increased up to 8 h. Biochemical changes induced by the different hormone treatments were studied by labelling the proteins with a 6-h pulse of [35S]methionine. The proteins present in the medium and in cells were analysed by two-dimensional polyacrylamide gel electrophoresis, followed by fluorography. Addition of oestrone sulphate alone or with progesterone produced a change in the patterns of cellular and secreted proteins compared with those in cells cultured with either oestradiol-17β or oestradiol-17β plus progesterone. Three cellular proteins (Mr < 14 000, isoelectric point (pI) 5·2 and 5·3; Mr 75 000, pI 4·9) and one secreted protein (Mr 155 000, pI 5·6–5·9) were specifically induced and could serve as markers of oestrone sulphate action. Journal of Endocrinology (1989) 123, 233–241

scholarly journals Phosphorylation of cellular proteins in Rous sarcoma virus-infected cells: analysis by use of anti-phosphotyrosine antibodies.

1988 ◽  
Vol 8 (8) ◽  
pp. 3035-3042 ◽  
Author(s):  
M Hamaguchi ◽  
C Grandori ◽  
H Hanafusa
Keyword(s):  
Gel Electrophoresis ◽  
Rous Sarcoma Virus ◽  
Cellular Proteins ◽  
Morphological Transformation ◽  
Protein Substrates ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Infected Cells ◽  
Avian Sarcoma ◽  
In Cells

The protein substrates for the tyrosine protein kinases in cells transformed by avian sarcoma viruses were analyzed by gel electrophoresis in combination with immunoblotting or immunoprecipitation by antibodies against phosphotyrosine. We found that greater than 90% of phosphotyrosine-containing cellular proteins can be immunoprecipitated by these antibodies. The level of phosphotyrosine-containing cellular proteins detectable by this method markedly increased upon transformation with Rous sarcoma virus, and more than 20 distinct bands of such proteins were found in lysates of Rous sarcoma virus-transformed cells. Most of these phosphotyrosine-containing proteins had not been identified by other methods, and their presence appeared to correlate with morphological transformation in cells infected with various Rous sarcoma virus mutants and Y73, PRCII, and Fujinami sarcoma viruses. However, considerably different patterns were obtained with cells infected with nontransforming Rous sarcoma virus mutants that encode nonmyristylated src kinases, indicating that most substrates that correlate with transformation can only be recognized by p60v-src associated with the plasma membrane.

scholarly journals Autophagy: Friend or Foe in Breast Cancer Development, Progression, and Treatment

2011 ◽  
Vol 2011 ◽  
pp. 1-7 ◽  
Author(s):  
Damian E. Berardi ◽  
Paola B. Campodónico ◽  
Maria Ines Díaz Bessone ◽  
Alejandro J. Urtreger ◽  
Laura B. Todaro
Keyword(s):  
Cell Death ◽  
Cell Survival ◽  
Anticancer Agents ◽  
Cancer Development ◽  
Nutrient Deprivation ◽  
Clinical Settings ◽  
Degradative Pathway ◽  
Autophagy Induction ◽  
Autophagy Inhibition ◽  
Catabolic Process

Autophagy is a catabolic process responsible for the degradation and recycling of long-lived proteins and organelles by lysosomes. This degradative pathway sustains cell survival during nutrient deprivation, but in some circumstances, autophagy leads to cell death. Thereby, autophagy can serve as tumor suppressor, as the reduction in autophagic capacity causes malignant transformation and spontaneous tumors. On the other hand, this process also functions as a protective cell-survival mechanism against environmental stress causing resistance to antineoplastic therapies. Although autophagy inhibition, combined with anticancer agents, could be therapeutically beneficial in some cases, autophagy induction by itself could lead to cell death in some apoptosis-resistant cancers, indicating that autophagy induction may also be used as a therapy. This paper summarizes the most important findings described in the literature about autophagy and also discusses the importance of this process in clinical settings.

scholarly journals p400 Is Required for E1A to Promote Apoptosis

2005 ◽  
Vol 280 (23) ◽  
pp. 21915-21923 ◽  
Author(s):  
Andrew V. Samuelson ◽  
Masako Narita ◽  
Ho-Man Chan ◽  
Jianping Jin ◽  
Elisa de Stanchina ◽  
...  
Keyword(s):  
Cell Death ◽  
Rna Interference ◽  
Chromatin Remodeling ◽  
Retinoblastoma Protein ◽  
Cellular Proteins ◽  
Creb Binding Protein ◽  
Adenovirus E1a ◽  
Chromatin Remodeling Complex ◽  
Cellular Machinery ◽  
Promote Cell Death

The adenovirus E1A oncoprotein promotes proliferation and transformation by binding cellular proteins, including members of the retinoblastoma protein family, the p300/CREB-binding protein transcriptional coactivators, and the p400-TRRAP chromatin-remodeling complex. E1A also promotes apoptosis, in part, by engaging the ARF-p53 tumor suppressor pathway. We show that E1A induces ARF and p53 and promotes apoptosis in normal fibroblasts by physically associating with the retinoblastoma protein and a p400-TRRAP complex and that its interaction with p300 is largely dispensable for these effects. We further show that E1A increases p400 expression and, conversely, that suppression of p400 using stable RNA interference reduces the levels of ARF, p53, and apoptosis in E1A-expressing cells. Therefore, whereas E1A inactivates the retinoblastoma protein, it requires p400 to efficiently promote cell death. These results identify p400 as a regulator of the ARF-p53 pathway and a component of the cellular machinery that couples proliferation to cell death.

scholarly journals Structural state recognition facilitates tip tracking of EB1 at growing microtubule ends in cells

2019 ◽  
Author(s):  
Taylor A. Reid ◽  
Courtney Coombes ◽  
Soumya Mukherjee ◽  
Rebecca R. Goldblum ◽  
Kyle White ◽  
...  
Keyword(s):  
Single Molecule ◽  
Cellular Proteins ◽  
Affinity Binding ◽  
Binding Model ◽  
State Recognition ◽  
High Affinity ◽  
Diffusion Limited ◽  
Quantitative Fluorescence ◽  
Closed Lattice ◽  
In Cells

AbstractThe microtubule binding protein EB1 specifically targets the growing ends of microtubules in cells, where EB1 facilitates the interactions of cellular proteins with microtubule plus-ends. Microtubule end targeting of EB1 has been attributed to high affinity binding of EB1 to GTP-tubulin that is present at growing microtubule ends. However, our 3D single-molecule diffusion simulations predicted a ∼6000% increase in EB1 arrivals to open, tapered microtubule tip structures relative to closed lattice conformations. Using quantitative fluorescence, single-molecule, and electron microscopy experiments, we found that the binding of EB1 onto opened, structurally disrupted microtubules was dramatically increased relative to closed, intact microtubules, regardless of hydrolysis state. Correspondingly, in cells, the conversion of growing microtubule ends from a tapered into a blunt configuration resulted in reduced EB1 targeting. Together, our results suggest that microtubule structural recognition, based on a fundamental diffusion-limited binding model, facilitates the tip tracking of EB1 at growing microtubule ends.

scholarly journals GRP78 enhances the glutamine metabolism to support cell survival from glucose deficiency by modulating the β-catenin signaling

Oncotarget ◽  
2014 ◽  
Vol 5 (14) ◽  
pp. 5369-5380 ◽  
Author(s):  
Zongwei Li ◽  
Yingying Wang ◽  
Haili Wu ◽  
Lichao Zhang ◽  
Peng Yang ◽  
...  
Keyword(s):  
Cell Survival ◽  
Glutamine Metabolism ◽  
Support Cell
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