PXD019537

PXD019537 is an original dataset announced via ProteomeXchange.

Title	3’,5’-cAMP affects actin cytoskeleton dynamics by direct binding to actin.
Description	Cyclic adenosine monophosphate (3’,5’-cAMP) is a well-characterized and evolutionary conserved second messenger. In contrast to the animal cells, however, the role of 3’,5’-cAMP in plants remains enigmatic. With the exception of cyclic nucleotide-gated ion channels, no plant 3’,5’-cAMP interactors have been reported to date. To address the existing gap, we resorted to thermal proteome profiling (TPP) as novel biochemical approach for the identification of protein binders of a small-molecule of choice. Based on the significant change in the thermal stability caused by 3’,5’-cAMP, we report a list of 51 putative 3’,5’-cAMP protein interactors, of which we focused on actin isovatriant ACT2. Most importantly we could demonstrate that 3’,5’-cAMP binding increases the rate of actin polymerization, resulting in longer actin filaments. Moreover, 3’,5’-cAMP treatment affected actin bundling, resulting in thicker actin bundles, as observed in the Arabidopsis hypocotyl cells. In line, with the obtained results 3’,5’-cAMP supplementation resulted in partial rescue of the short hypocotyl phenotype of the act2act7 Arabidopsis mutant, and 3’,5’-cAMP treatment suppressed actin depolymerization induced by Latrunculin B. Finally, 3’,5’-cAMP effects were independent from its degradation to adenosine, and true for nanomolar concentrations of 3’,5’-cAMP reported for the plant cells. Considering evolutionary conservation of 3’,5’-cAMP and actin we expect that our findings will be relevant to other eukaryotic organisms, and as such demonstrate a novel and direct mechanism of 3’,5’-cAMP regulation of the actin cytoskeleton dynamics.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:48:26.088.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Marcin Luzarowski
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	phosphorylated residue; monohydroxylated residue; acetylated residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2020-06-03 01:03:42	ID requested
1	2023-06-02 05:26:28	announced
⏵ 2	2023-11-14 08:48:29	announced	2023-11-14: Updated project metadata.

Figueroa NE, Franz P, Luzarowski M, Martinez-Seidel F, Moreno JC, Childs D, Ziemblicka A, Sampathkumar A, Andersen TG, Tsiavaliaris G, Chodasiewicz M, Skirycz A, Protein interactome of 3',5'-cAMP reveals its role in regulating the actin cytoskeleton. Plant J, 115(5):1214-1230(2023) [pubmed]

submitter keyword: cAMP,actin, cytoskeleton, Arabidopsis thaliana, signalling

Aleksandra Skirycz
contact affiliation	Max-Planck-Institute of Molecular Plant Physiology, Golm, Germany
contact email	skirycz@mpimp-golm.mpg.de
lab head
Marcin Luzarowski
contact affiliation	University of Heidelberg
contact email	m.luzarowski@zmbh.uni-heidelberg.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2023/06/PXD019537

PRIDE project URI

• PRIDE
  1. PXD019537
     1. Label: PRIDE project
     2. Name: 3’,5’-cAMP affects actin cytoskeleton dynamics by direct binding to actin.