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Main Authors: Xu, Jia, Zhang, Yongli, Pan, Junmin
Format: Artículo científico
Language:en
Published: FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2025
Subjects:
Online Access:https://pubmed.ncbi.nlm.nih.gov/40948379/
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author Xu, Jia
Zhang, Yongli
Pan, Junmin
author_facet Xu, Jia
Zhang, Yongli
Pan, Junmin
Xu, Jia
Zhang, Yongli
Pan, Junmin
collection PubMed - marine biology
contents Primary Cilia-Mediated Hedgehog Signaling Regulates Cell Fate During ER Stress-Induced Life or Death Decisions. Xu, Jia Zhang, Yongli Pan, Junmin Cilia Endoplasmic Reticulum Stress Hedgehog Proteins Animals Signal Transduction Mice Humans Unfolded Protein Response Smoothened Receptor Cholesterol eIF-2 Kinase Protein Serine-Threonine Kinases Primary cilia play critical roles in development and physiology. The unfolded protein response (UPR), triggered by endoplasmic reticulum (ER) stress, is a fundamental cellular process. However, whether and how ER stress influences ciliary assembly and function remain poorly understood. Here, we demonstrate that ER stress promotes ciliogenesis and hedgehog (HH) signaling by upregulating cholesterol levels, thereby alleviating cellular damage. IRE1 and PERK, sensors of ER stress, positively regulate ciliogenesis by enhancing the trafficking of preciliary vesicles through upregulation of cellular cholesterol levels via activation of SREBP2. Furthermore, the cholesterol content in the ciliary membrane also increases during ER stress, leading to enhanced ciliary recruitment of Smoothened (SMO) and activation of HH signaling. The activation of HH signaling via primary cilium is crucial for protecting cells from stress-induced damage. Our findings unveil a pivotal role of cilia-mediated hedgehog signaling in cell fate determination under ER stress.
format Artículo científico
id pubmed_40948379
institution PubMed
language en
publishDate 2025
publisher FASEB journal : official publication of the Federation of American Societies for Experimental Biology
record_format pubmed
spellingShingle Primary Cilia-Mediated Hedgehog Signaling Regulates Cell Fate During ER Stress-Induced Life or Death Decisions.
Xu, Jia
Zhang, Yongli
Pan, Junmin
Cilia
Endoplasmic Reticulum Stress
Hedgehog Proteins
Animals
Signal Transduction
Mice
Humans
Unfolded Protein Response
Smoothened Receptor
Cholesterol
eIF-2 Kinase
Protein Serine-Threonine Kinases
Primary Cilia-Mediated Hedgehog Signaling Regulates Cell Fate During ER Stress-Induced Life or Death Decisions. Xu, Jia Zhang, Yongli Pan, Junmin Cilia Endoplasmic Reticulum Stress Hedgehog Proteins Animals Signal Transduction Mice Humans Unfolded Protein Response Smoothened Receptor Cholesterol eIF-2 Kinase Protein Serine-Threonine Kinases Primary cilia play critical roles in development and physiology. The unfolded protein response (UPR), triggered by endoplasmic reticulum (ER) stress, is a fundamental cellular process. However, whether and how ER stress influences ciliary assembly and function remain poorly understood. Here, we demonstrate that ER stress promotes ciliogenesis and hedgehog (HH) signaling by upregulating cholesterol levels, thereby alleviating cellular damage. IRE1 and PERK, sensors of ER stress, positively regulate ciliogenesis by enhancing the trafficking of preciliary vesicles through upregulation of cellular cholesterol levels via activation of SREBP2. Furthermore, the cholesterol content in the ciliary membrane also increases during ER stress, leading to enhanced ciliary recruitment of Smoothened (SMO) and activation of HH signaling. The activation of HH signaling via primary cilium is crucial for protecting cells from stress-induced damage. Our findings unveil a pivotal role of cilia-mediated hedgehog signaling in cell fate determination under ER stress.
title Primary Cilia-Mediated Hedgehog Signaling Regulates Cell Fate During ER Stress-Induced Life or Death Decisions.
topic Cilia
Endoplasmic Reticulum Stress
Hedgehog Proteins
Animals
Signal Transduction
Mice
Humans
Unfolded Protein Response
Smoothened Receptor
Cholesterol
eIF-2 Kinase
Protein Serine-Threonine Kinases
url https://pubmed.ncbi.nlm.nih.gov/40948379/