Rasd1 modulates the coactivator function of NonO in the cyclic AMP pathway.

All living organisms exhibit autonomous daily physiological and behavioural rhythms to help them synchronize with the environment. Entrainment of circadian rhythm is achieved via activation of cyclic AMP (cAMP) and mitogen-activated protein kinase signaling pathways. NonO (p54nrb) is a multifunction...

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Autores principales:	Shufen Angeline Ong, Jen Jen Tan, Wai Loon Tew, Ken-Shiung Chen
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/4d0dbe846e824bf892dd7c207b0d3ca3
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spelling	oai:doaj.org-article:4d0dbe846e824bf892dd7c207b0d3ca32021-11-18T06:46:33ZRasd1 modulates the coactivator function of NonO in the cyclic AMP pathway.1932-620310.1371/journal.pone.0024401https://doaj.org/article/4d0dbe846e824bf892dd7c207b0d3ca32011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21915321/?tool=EBIhttps://doaj.org/toc/1932-6203All living organisms exhibit autonomous daily physiological and behavioural rhythms to help them synchronize with the environment. Entrainment of circadian rhythm is achieved via activation of cyclic AMP (cAMP) and mitogen-activated protein kinase signaling pathways. NonO (p54nrb) is a multifunctional protein involved in transcriptional activation of the cAMP pathway and is involved in circadian rhythm control. Rasd1 is a monomeric G protein implicated to play a pivotal role in potentiating both photic and nonphotic responses of the circadian rhythm. In this study, we have identified and validated NonO as an interacting partner of Rasd1 via affinity pulldown, co-immunoprecipitation and indirect immunofluorescence studies. The GTP-hydrolysis activity of Rasd1 is required for the functional interaction. Functional interaction of Rasd1-NonO in the cAMP pathway was investigated via reporter gene assays, chromatin immunoprecipitation and gene knockdown. We showed that Rasd1 and NonO interact at the CRE-site of specific target genes. These findings reveal a novel mechanism by which the coregulator activity of NonO can be modulated.Shufen Angeline OngJen Jen TanWai Loon TewKen-Shiung ChenPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 9, p e24401 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Shufen Angeline Ong Jen Jen Tan Wai Loon Tew Ken-Shiung Chen Rasd1 modulates the coactivator function of NonO in the cyclic AMP pathway.
description	All living organisms exhibit autonomous daily physiological and behavioural rhythms to help them synchronize with the environment. Entrainment of circadian rhythm is achieved via activation of cyclic AMP (cAMP) and mitogen-activated protein kinase signaling pathways. NonO (p54nrb) is a multifunctional protein involved in transcriptional activation of the cAMP pathway and is involved in circadian rhythm control. Rasd1 is a monomeric G protein implicated to play a pivotal role in potentiating both photic and nonphotic responses of the circadian rhythm. In this study, we have identified and validated NonO as an interacting partner of Rasd1 via affinity pulldown, co-immunoprecipitation and indirect immunofluorescence studies. The GTP-hydrolysis activity of Rasd1 is required for the functional interaction. Functional interaction of Rasd1-NonO in the cAMP pathway was investigated via reporter gene assays, chromatin immunoprecipitation and gene knockdown. We showed that Rasd1 and NonO interact at the CRE-site of specific target genes. These findings reveal a novel mechanism by which the coregulator activity of NonO can be modulated.
format	article
author	Shufen Angeline Ong Jen Jen Tan Wai Loon Tew Ken-Shiung Chen
author_facet	Shufen Angeline Ong Jen Jen Tan Wai Loon Tew Ken-Shiung Chen
author_sort	Shufen Angeline Ong
title	Rasd1 modulates the coactivator function of NonO in the cyclic AMP pathway.
title_short	Rasd1 modulates the coactivator function of NonO in the cyclic AMP pathway.
title_full	Rasd1 modulates the coactivator function of NonO in the cyclic AMP pathway.
title_fullStr	Rasd1 modulates the coactivator function of NonO in the cyclic AMP pathway.
title_full_unstemmed	Rasd1 modulates the coactivator function of NonO in the cyclic AMP pathway.
title_sort	rasd1 modulates the coactivator function of nono in the cyclic amp pathway.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/4d0dbe846e824bf892dd7c207b0d3ca3
work_keys_str_mv	AT shufenangelineong rasd1modulatesthecoactivatorfunctionofnonointhecyclicamppathway AT jenjentan rasd1modulatesthecoactivatorfunctionofnonointhecyclicamppathway AT wailoontew rasd1modulatesthecoactivatorfunctionofnonointhecyclicamppathway AT kenshiungchen rasd1modulatesthecoactivatorfunctionofnonointhecyclicamppathway
_version_	1718424412312567808

Rasd1 modulates the coactivator function of NonO in the cyclic AMP pathway.

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