PXD046497

PXD046497 is an original dataset announced via ProteomeXchange.

Title	SEPT6 affinity purification-mass spectrometry (AP-MS)
Description	Septin proteins interact intermolecularly to form hetero-oligomeric complexes that further assemble into higher-order filaments. To investigate whether the interactions among septin proteins are affected by RID, we conducted affinity purification-mass spectrometry (AP-MS) experiments. In this regard, EGFP-tagged SEPT6 or its quadruple mutant SEPT6-4KR was co-expressed with RID-WT or RID-CA in cells and immunoprecipitated by anti-EGFP beads. The resulting co-immunoprecipitates were analyzed and compared with the vector control by label-free quantitative (LFQ) proteomics to identify and quantify septin proteins associated with SEPT6. The MS analysis showed that SEPT6 were indeed co-affinity-purified with all endogenous septin proteins that were identified, such as SEPT2, SEPT3, SEPT5, SEPT6, SEPT7, SEPT8, SEPT9, SEPT10, and SEPT11, in the absence of RID activity. More importantly, the interactions between SEPT6 and these septins were not affected by RID-WT expression. Interestingly, the SEPT6-4KR mutant could still interact and likely form heteromeric complexes with other fatty-acylated septin proteins (e.g., SEPT2, SEPT3, SEPT5, SEPT6, SEPT7, SEPT8, SEPT9, SEPT10 and SEPT11) in the presence of RID activity.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_06:46:28.763.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Tao Peng
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	iodoacetamide derivatized residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2023-10-30 03:39:41	ID requested
1	2024-06-22 08:42:58	announced
⏵ 2	2024-10-22 06:46:29	announced	2024-10-22: Updated project metadata.

10.1016/j.mcpro.2024.100730;

Xu Y, Ding K, Peng T, -Fatty-Acylation of Septins by Rho Inactivation Domain (RID) of the Vibrio MARTX Toxin to Alter Septin Localization and Organization. Mol Cell Proteomics, 23(3):100730(2024) [pubmed]

submitter keyword: SEPT6, RID, fatty-acylation

Tao Peng
contact affiliation	Peking University Graduate School
contact email	tpeng@pku.edu.cn
lab head
Tao Peng
contact affiliation	Peking University Shenzhen Graduate School
contact email	penglab@yeah.net
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD046497
     1. Label: PRIDE project
     2. Name: SEPT6 affinity purification-mass spectrometry (AP-MS)