TY - JOUR
T1 - The RNA-binding protein HuR promotes cell migration and cell invasion by stabilizing the β-actin mRNA in a U-rich-element-dependent manner
AU - Dormoy-Raclet, Virginie
AU - Ménard, Isabelle
AU - Clair, Eveline
AU - Kurban, Ghada
AU - Mazroui, Rachid
AU - Di Marco, Sergio
AU - Von Roretz, Christopher
AU - Pause, Arnim
AU - Gallouzi, Imed Eddine
N1 - Generated from Scopus record by KAUST IRTS on 2022-09-13
PY - 2007/8/1
Y1 - 2007/8/1
N2 - A high expression level of the β-actin protein is required for important biological mechanisms, such as maintaining cell shape, growth, and motility. Although the elevated cellular level of the β-actin protein is directly linked to the long half-life of its mRNA, the molecular mechanisms responsible for this effect are unknown. Here we show that the RNA-binding protein HuR stabilizes the β-actin mRNA by associating with a uridine-rich element within its 3′ untranslated region. Using RNA interference to knock down the expression of HuR in HeLa cells, we demonstrate that HuR plays an important role in the stabilization but not in the nuclear/cytoplasmic distribution of the β-actin mRNA. HuR depletion in HeLa cells alters key β-actin-based cytoskeleton functions, such as cell adhesion, migration, and invasion, and these defects correlate with a loss of the actin stress fiber network. Together our data establish that the posttranscriptional event involving HuR-mediated β-actin mRNA stabilization could be a part of the regulatory mechanisms responsible for maintaining cell integrity, which is a prerequisite for avoiding transformation and tumor formation. Copyright © 2007, American Society for Microbiology. All Rights Reserved.
AB - A high expression level of the β-actin protein is required for important biological mechanisms, such as maintaining cell shape, growth, and motility. Although the elevated cellular level of the β-actin protein is directly linked to the long half-life of its mRNA, the molecular mechanisms responsible for this effect are unknown. Here we show that the RNA-binding protein HuR stabilizes the β-actin mRNA by associating with a uridine-rich element within its 3′ untranslated region. Using RNA interference to knock down the expression of HuR in HeLa cells, we demonstrate that HuR plays an important role in the stabilization but not in the nuclear/cytoplasmic distribution of the β-actin mRNA. HuR depletion in HeLa cells alters key β-actin-based cytoskeleton functions, such as cell adhesion, migration, and invasion, and these defects correlate with a loss of the actin stress fiber network. Together our data establish that the posttranscriptional event involving HuR-mediated β-actin mRNA stabilization could be a part of the regulatory mechanisms responsible for maintaining cell integrity, which is a prerequisite for avoiding transformation and tumor formation. Copyright © 2007, American Society for Microbiology. All Rights Reserved.
UR - https://journals.asm.org/doi/10.1128/MCB.00113-07
UR - http://www.scopus.com/inward/record.url?scp=34547235597&partnerID=8YFLogxK
U2 - 10.1128/MCB.00113-07
DO - 10.1128/MCB.00113-07
M3 - Article
SN - 0270-7306
VL - 27
SP - 5365
EP - 5380
JO - Molecular and Cellular Biology
JF - Molecular and Cellular Biology
IS - 15
ER -