PXD015431-2

PXD015431 is an original dataset announced via ProteomeXchange.

Title	ADAM17 cytoplasmic domain modulates Thioredoxin-1 conformation and activity
Description	We have demonstrated that site-directed mutagenesis in ADAM17 (ADAM17cytoF730A) also disrupts the interacting interface with Trx-1, resulting in a decrease of Trx-1 reductive capacity and activity. One of the mechanisms that explain this effect might be that ADAM17cyto favors Trx-1 monomerization state - the active state - by forming a disulfide bond between Cys824 at the C-terminal of ADAM17cyto with the Cys73 of Trx-1, which is involved in the dimerization site. Moreover, we observed that ADAM17 overexpressing or knockdown cells favors or not the monomeric state of Trx-1, respectively. As a result, there is a decrease of oxidant levels and ADAM17 sheddase activity, and an increase in the reduced cysteine-containing peptides in intracellular proteins in ADAM17cyto overexpressing cells. In summary, we propose that ADAM17 is able to modulate Trx-1 conformation affecting its activity and intracellular redox state.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:13:36.188.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Adriana Franco Paes Leme
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2019-09-12 08:36:31	ID requested
1	2020-10-18 23:51:49	announced
⏵ 2	2024-10-22 05:13:42	announced	2024-10-22: Updated project metadata.

10.1016/j.redox.2020.101735;

E Costa RAP, Granato DC, Trino LD, Yokoo S, Carnielli CM, Kawahara R, Domingues RR, Pauletti BA, Neves LX, Santana AG, Paulo JA, Arag, ã, o AZB, Heleno Batista FA, Migliorini Figueira AC, Laurindo FRM, Fernandes D, Hansen HP, Squina F, Gygi SP, Paes Leme AF, ADAM17 cytoplasmic domain modulates Thioredoxin-1 conformation and activity. Redox Biol, 37():101735(2020) [pubmed]

submitter keyword: ADAM17, Thioredoxin-1, mass spectrometry, redox signaling., dimerization, iodoTMT

Adriana Franco Paes Leme
contact affiliation	National Laboratory of Biosciences (LNBio), CNPEM, Brazil.
contact email	adriana.paesleme@lnbio.cnpem.br
lab head
Adriana Franco Paes Leme
contact affiliation	CNPEM
contact email	adriana.paesleme@lnbio.cnpem.br
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/2020/10/PXD015431

PRIDE project URI

• PRIDE
  1. PXD015431
     1. Label: PRIDE project
     2. Name: ADAM17 cytoplasmic domain modulates Thioredoxin-1 conformation and activity