Kiely_2016_activation.pdf (1.88 MB)
Download fileActivation of the cAMP pathway induces RACK1-Dependent binding of β-Actin to BDNF promoter
journal contribution
posted on 2022-11-29, 12:45 authored by Jeremie Neasta, Anna Fiorenza, Dao-Yao He, Khanhky Phamluong, PATRICK KIELYPATRICK KIELYRACK1 is a scaffolding protein that contributes to the specificity and propagation of several
signaling cascades including the cAMP pathway. As such, RACK1 participates in numerous
cellular functions ranging from cell migration and morphology to gene transcription. To
obtain further insights on the mechanisms whereby RACK1 regulates cAMP-dependent
processes, we set out to identify new binding partners of RACK1 during activation of the
cAMP signaling using a proteomics strategy. We identified β-actin as a direct RACK1 binding
partner and found that the association between β-actin and RACK1 is increased in
response to the activation of the cAMP pathway. Furthermore, we show that cAMP-dependent
increase in BDNF expression requires filamentous actin. We further report that β-actin
associates with the BDNF promoter IV upon the activation of the cAMP pathway and present
data to suggest that the association of β-actin with BDNF promoter IV is RACK1-dependent.
Taken together, our data suggest that β-actin is a new RACK1 binding partner and
that the RACK1 and β-actin association participate in the cAMP-dependent regulation of
BDNF transcription.
History
Publication
PloS One;Publisher
Public Library of ScienceNote
peer-reviewedOther Funding information
National Institutes of Health (NIH), SFILanguage
EnglishAlso affiliated with
- Bernal Institute
External identifier
Department or School
- School of Medicine