PXD029704

PXD029704 is an original dataset announced via ProteomeXchange.

Title	Intricate coupling between the transactivation and basic-leucine zipper domains governs the CK2-dependent phosphorylation of ATF4
Description	Most transcription factors possess at least one long intrinsically disordered transactivation domain that binds to a variety of co-activators and co-repressors and plays a key role in modulating the transcriptional activity. Despite the crucial importance of these mechanisms, the structural and functional basis of transactivation domain in yet poorly understood. Here, we focused on ATF4/CREB-2, an essential transcription factor for cellular stress adaptation. We found that the N-terminal region of the transactivation domain is involved in transient long-range interactions with the basic-leucine zipper domain. In vitro phosphorylation assays with the protein kinase CK2 show that the presence of the basic-leucine zipper domain is required for optimal phosphorylation of the transactivation domain. This study uncovers the intricate coupling existing between the transactivation and basic-leucine zipper domains of ATF4 and highlights its potential functional relevance.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:37:50.243.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Steven Siang
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	phosphorylated residue; monohydroxylated residue; deamidated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2021-11-12 06:06:26	ID requested
1	2023-03-10 23:07:39	announced
⏵ 2	2023-11-14 08:37:51	announced	2023-11-14: Updated project metadata.

Siang S, Underbakke ES, Roche J, Intricate coupling between the transactivation and basic-leucine zipper domains governs phosphorylation of transcription factor ATF4 by casein kinase 2. J Biol Chem, 298(3):101633(2022) [pubmed]

submitter keyword: ATF4, intrinsically disordered domain, phosphorylation,LC-MSMS

Julien Roche
contact affiliation	Roy J. Carver Dept. of Biochemistry, Biophysics, and Molecular Biology Iowa State University Ames, Iowa, USA
contact email	jroche@iastate.edu
lab head
Steven Siang
contact affiliation	Iowa State University
contact email	ssiang@iastate.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD029704
     1. Label: PRIDE project
     2. Name: Intricate coupling between the transactivation and basic-leucine zipper domains governs the CK2-dependent phosphorylation of ATF4