YAP1 and PRDM14 converge to promote cell survival and tumorigenesis

2022 ◽  
Author(s):  
Miju Kim ◽  
Seav Huong Ly ◽  
Yingtian Xie ◽  
Gina N. Duronio ◽  
Dane Ford-Roshon ◽  
...  
Keyword(s):  
Cell Survival ◽  
Promote Cell Survival

Integrin α8β1–fibronectin interactions promote cell survival via PI3 kinase pathway

2005 ◽  
Vol 329 (1) ◽  
pp. 305-311 ◽  
Author(s):  
Eduardo Farias ◽  
Min Lu ◽  
Xianwu Li ◽  
Lynn M. Schnapp
Keyword(s):  
Cell Survival ◽  
Pi3 Kinase ◽  
Promote Cell Survival ◽  
Pi3 Kinase Pathway ◽  
Kinase Pathway

Kinase cascades regulating entry into apoptosis

1997 ◽  
Vol 61 (1) ◽  
pp. 33-46
Author(s):  
P Anderson
Keyword(s):  
Cell Death ◽  
Cell Surface ◽  
Cell Survival ◽  
Tyrosine Kinases ◽  
Uv Light ◽  
Apoptotic Cell ◽  
Paracrine Factors ◽  
Surface Receptors ◽  
Promote Cell Survival ◽  
Necrosis Factor

All cells are constantly exposed to conflicting environment cues that signal cell survival or cell death. Survival signals are delivered by autocrine or paracrine factors that actively suppress a default death pathway. In addition to survival factor withdrawal, cell death can be triggered by environmental stresses such as heat, UV light, and hyperosmolarity or by dedicated death receptors (e.g., FAS/APO-1 and tumor necrosis factor [TNF] receptors) that are counterparts of growth factor or survival receptors at the cell surface. One of the ways that cells integrate conflicting exogenous stimuli is by phosphorylation (or dephosphorylation) of cellular constituents by interacting cascades of serine/threonine and tyrosine protein kinases (and phosphatases). Survival factors (e.g., growth factors and mitogens) activate receptor tyrosine kinases and selected mitogen-activated, cyclin-dependent, lipid-activated, nucleic acid-dependent, and cyclic AMP-dependent kinases to promote cell survival and proliferation, whereas environmental stress (or death factors such as FAS/APO-1 ligand and TNF-alpha) activates different members of these kinase families to inhibit cell growth and, under some circumstances, promote apoptotic cell death. Because individual kinase cascades can interact with one another, they are able to integrate conflicting exogenous stimuli and provide a link between cell surface receptors and the biochemical pathways leading to cell proliferation or cell death.

Oncogenic H-Ras and PI3K signaling can inhibit E-cadherin-dependent apoptosis and promote cell survival after photodynamic therapy in mouse keratinocytes

2009 ◽  
Vol 219 (1) ◽  
pp. 84-93 ◽  
Author(s):  
Jesús Espada ◽  
Sergio Galaz ◽  
Francisco Sanz-Rodríguez ◽  
Alfonso Blázquez-Castro ◽  
Juan Carlos Stockert ◽  
...  
Keyword(s):  
Photodynamic Therapy ◽  
Cell Survival ◽  
Pi3k Signaling ◽  
Promote Cell Survival ◽  
Mouse Keratinocytes ◽  
E Cadherin

scholarly journals Death Receptor-Induced Activation of Initiator Caspase 8 Is Antagonized by Serine/Threonine Kinase PAK4

2003 ◽  
Vol 23 (21) ◽  
pp. 7838-7848 ◽  
Author(s):  
Nerina Gnesutta ◽  
Audrey Minden
Keyword(s):  
Cell Death ◽  
Cell Survival ◽  
Intracellular Signaling ◽  
Death Receptor ◽  
Caspase 8 ◽  
Death Domain ◽  
Serine Threonine Kinase ◽  
Threonine Kinase ◽  
Different Types ◽  
Promote Cell Survival

ABSTRACT Normal cell growth requires a precisely controlled balance between cell death and survival. This involves activation of different types of intracellular signaling cascades within the cell. While some types of signaling proteins regulate apoptosis, or programmed cell death, other proteins within the cell can promote survival. The serine/threonine kinase PAK4 can protect cells from apoptosis in response to several different types of stimuli. As is the case for other members of the p21-activated kinase (PAK) family, one way that PAK4 may promote cell survival is by phosphorylating and thereby inhibiting the proapoptotic protein Bad. This leads in turn to the inhibition of effector caspases such as caspase 3. Here we show that in response to cytokines which activate death domain-containing receptors, such as the tumor necrosis factor and Fas receptors, PAK4 can inhibit the death signal by a different mechanism. Under these conditions, PAK4 inhibits apoptosis early in the caspase cascade, antagonizing the activation of initiator caspase 8. This inhibition, which does not require PAK4's kinase activity, may involve inhibition of caspase 8 recruitment to the death domain receptors. This role in regulating initiator caspases is an entirely novel role for the PAK proteins and suggests a new mechanism by which these proteins promote cell survival.

scholarly journals Dengue activates mTORC2 signaling to counteract apoptosis and maximize viral replication

2020 ◽  
Author(s):  
Christoph C. Carter ◽  
Jean Paul Olivier ◽  
Alexis Kaushansky ◽  
Fred D. Mast ◽  
John D. Aitchison
Keyword(s):  
Viral Replication ◽  
Cell Survival ◽  
Structural Protein ◽  
Protein Protein Interaction ◽  
Mechanistic Target Of Rapamycin ◽  
Promote Cell Survival ◽  
Important Regulator ◽  
Infected Cells ◽  
Induced Apoptosis

ABSTRACTThe mechanistic target of rapamycin (mTOR) functions in at least two distinct complexes: mTORC1, which regulates cellular anabolic-catabolic homeostasis, and mTORC2, which is an important regulator of cell survival and cytoskeletal maintenance. mTORC1 has been implicated in the pathogenesis of flaviviruses including dengue, where it contributes to the establishment of a pro-viral autophagic state. In contrast, the role of mTORC2 in viral pathogenesis is unknown. In this study, we explore the consequences of a physical protein-protein interaction between dengue non-structural protein 5 (NS5) and host cell mTOR proteins during infection. Using shRNA to differentially target mTORC1 and mTORC2 complexes, we show that mTORC2 is required for optimal dengue replication. Furthermore, we show that mTORC2 is activated during viral replication, and that mTORC2 counteracts virus-induced apoptosis, promoting the survival of infected cells. This work reveals a novel mechanism by which the dengue flavivirus can promote cell survival to maximize viral replication.

scholarly journals A Short Tandem Repeat-Enriched RNA Assembles a Nuclear Compartment to Control Alternative Splicing and Promote Cell Survival

2018 ◽  
Vol 72 (3) ◽  
pp. 525-540.e13 ◽  
Author(s):  
Karen Yap ◽  
Svetlana Mukhina ◽  
Gen Zhang ◽  
Jason S.C. Tan ◽  
Hong Sheng Ong ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Cell Survival ◽  
Tandem Repeat ◽  
Short Tandem Repeat ◽  
Nuclear Compartment ◽  
Promote Cell Survival ◽  
Short Tandem

scholarly journals Neuronal Calcium Sensor 1 is up‐regulated in response to stress to promote cell survival and motility in cancer cells

2020 ◽  
Vol 14 (6) ◽  
pp. 1134-1151
Author(s):  
Henrike K. Grosshans ◽  
Tom T. Fischer ◽  
Julia A. Steinle ◽  
Allison L. Brill ◽  
Barbara E. Ehrlich
Keyword(s):  
Cell Survival ◽  
Cancer Cells ◽  
Calcium Sensor ◽  
Neuronal Calcium Sensor ◽  
Promote Cell Survival ◽  
Response To Stress

scholarly journals Pax2/5/8 proteins promote cell survival in C. elegans

Development ◽  
2006 ◽  
Vol 133 (21) ◽  
pp. 4193-4202 ◽  
Author(s):  
D. Park ◽  
H. Jia ◽  
V. Rajakumar ◽  
H. M. Chamberlin
Keyword(s):  
Cell Survival ◽  
C Elegans ◽  
Promote Cell Survival
Sign in / Sign up

Export Citation Format

Share Document