Cellular stress responses Archives - Laboratory Notes

ATF6

admin — Sat, 29 Aug 2026 09:58:21 +0000

ATF6 is an ER stress‑responsive transcription factor that enhances protein‑folding capacity and strengthens ER‑associated degradation. After trafficking to the Golgi and undergoing regulated proteolysis, ATF6 activates genes that restore ER proteostasis during unfolded protein accumulation.

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Apoptosis

admin — Sat, 29 Aug 2026 09:51:15 +0000

Apoptosis is a controlled form of programmed cell death that removes damaged or unnecessary cells without causing inflammation. Through coordinated activation of extrinsic and intrinsic pathways, apoptosis maintains tissue homeostasis and protects organisms from disease.

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Endoplasmic Reticulum Stress

admin — Sat, 29 Aug 2026 09:50:51 +0000

ER stress arises when misfolded proteins accumulate in the endoplasmic reticulum, overwhelming its folding capacity. Through IRE1, PERK and ATF6 signalling, the unfolded protein response restores proteostasis, reduces protein load and protects cells from stress‑induced damage.

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Ferroptosis

admin — Sat, 29 Aug 2026 09:42:47 +0000

Ferroptosis is a regulated form of cell death characterised by iron‑dependent lipid peroxidation and catastrophic membrane damage. Unlike apoptosis, necroptosis...

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Programmed Cell Death

admin — Sat, 29 Aug 2026 09:14:14 +0000

Programmed cell death (PCD) is a regulated biological process that eliminates damaged or unnecessary cells through apoptosis, autophagic cell death and regulated necrosis. By maintaining tissue homeostasis and supporting stress adaptation, PCD is essential for development and long‑term organismal health.

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Necroptosis

admin — Fri, 28 Aug 2026 10:33:18 +0000

Necroptosis is a regulated necrotic cell‑death pathway driven by RIPK1–RIPK3–MLKL signalling. Through membrane permeabilisation and inflammatory activation, necroptosis eliminates infected or damaged cells when apoptosis is blocked, shaping immunity and disease progression.

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RIPK1

admin — Fri, 28 Aug 2026 10:19:09 +0000

RIPK1 is a central signalling kinase that determines whether a cell survives, undergoes apoptosis or triggers necroptosis. Through context‑dependent interactions with TNFR1, caspase‑8, RIPK3 and MLKL, RIPK1 integrates inflammatory cues and stress signals to regulate cell fate.

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RIPK3

admin — Fri, 28 Aug 2026 10:03:07 +0000

RIPK3 is a central necroptotic kinase that phosphorylates MLKL and drives regulated necrotic cell death. Through necrosome formation with RIPK1 and activation of inflammatory signalling, RIPK3 shapes immunity, tissue injury and disease progression.

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MLKL

admin — Thu, 27 Aug 2026 22:38:31 +0000

MLKL is the terminal effector of necroptosis. After phosphorylation by RIPK3, MLKL oligomerises and inserts into the plasma membrane, causing membrane rupture and release of inflammatory DAMPs. MLKL is essential for regulated necrotic cell death and immune activation.

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Endoplasmic Reticulum Associated Degradation

admin — Thu, 27 Aug 2026 00:18:51 +0000

ERAD is a central ER quality‑control pathway that recognises misfolded proteins, retrotranslocates them to the cytosol, ubiquitinates them and directs them to the proteasome. By preventing proteotoxic accumulation, ERAD preserves ER homeostasis and supports cellular proteostasis.

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PERK

admin — Thu, 27 Aug 2026 00:05:54 +0000

PERK is a central ER stress sensor that phosphorylates eIF2α, reduces protein synthesis and activates ATF4‑dependent transcription. Through adaptive and apoptotic signalling, PERK coordinates unfolded protein response pathways that restore proteostasis or eliminate irreparably damaged cells.

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IRE1

admin — Thu, 27 Aug 2026 00:01:37 +0000

IRE1 is the most conserved ER stress sensor, activating XBP1 splicing and RIDD to restore proteostasis. Through its kinase and RNase activities, IRE1 detects misfolded proteins, initiates adaptive signalling and coordinates the unfolded protein response during ER stress.

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Proteostasis Network

admin — Wed, 26 Aug 2026 23:35:50 +0000

The proteostasis network is an integrated system of chaperones, degradation pathways and organelle‑specific quality‑control mechanisms that maintains protein folding, stability and function. By coordinating refolding, repair and degradation, cells prevent proteotoxic stress and preserve homeostasis.

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Unfolded Protein Response

admin — Wed, 26 Aug 2026 23:29:46 +0000

The unfolded protein response (UPR) is a conserved ER stress pathway that detects misfolded proteins and restores proteostasis. Through IRE1, PERK and ATF6 signalling, cells expand folding capacity, reduce protein load and maintain homeostasis under conditions of ER stress.

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Heat Shock Response

admin — Wed, 26 Aug 2026 23:24:31 +0000

The heat‑shock response (HSR) is a conserved cellular defence pathway that protects the proteome under stress. By activating HSF1 and inducing heat‑shock proteins, cells stabilise protein folding, prevent aggregation and restore proteostasis during proteotoxic conditions.

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Oxidative Stress Response

admin — Wed, 26 Aug 2026 23:09:10 +0000

The oxidative stress response is a cellular defence system that neutralises reactive oxygen species (ROS) and restores redox balance. Through antioxidant enzymes, Nrf2‑mediated transcription, mitochondrial regulation and damage‑repair pathways, cells protect themselves from oxidative injury and maintain homeostasis.

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Cellular Stress Response

admin — Wed, 26 Aug 2026 22:19:52 +0000

Cellular stress responses are adaptive defence mechanisms that protect cells from environmental, metabolic and proteotoxic stress. By activating heat‑shock proteins, unfolded protein responses, antioxidant pathways and autophagy, cells restore homeostasis and maintain functional integrity under adverse conditions.

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Protein Quality Control

admin — Wed, 26 Aug 2026 00:02:22 +0000

Protein quality control (PQC) is a cellular surveillance system that preserves proteome integrity by monitoring protein folding, repairing misfolded proteins and eliminating damaged or aggregated species. Through coordinated action of chaperones, the ubiquitin–proteasome system and autophagy, PQC protects cells from proteotoxic stress and maintains homeostasis.

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