PXD015431

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	2020-10-19
AnnouncementXML	Submission_2020-10-18_23:51:48.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

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, dimerization, mass spectrometry, iodoTMT, redox signaling.

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

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PRIDE project URI

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