PXD001353

PXD001353 is an original dataset announced via ProteomeXchange.

Title	Truncated Tau
Description	Tau is a microtubule-associated protein that ensures neuronal shape and function. Besides, Tau is a central player in Alzheimer’s disease (AD) and related Tauopathies where it is found aggregated in degenerating neurons. Mechanisms leading to Tau pathology and its progression are far from being elucidated. Among Tau species found in AD brains, several yet unidentified truncated Tau fragments are showed. A major step forward in the understanding of the role of Tau truncation would be to identify the precise cleavage sites of Tau species. This key step is mandatory to generate appropriate experimental tools in order to investigate the impact of each identified truncated-species on Tau function/dysfunction. Here, we achieved an optimized proteomics approach and succeed in identifying a number of new N-terminally truncated-Tau species from human brain. As N-terminal residues of these fragments are located broadly across Tau sequence, one could expect to have different effects on Tau. We initiated cell-based functional studies by analyzing biochemical characteristics of two N-terminally truncated Tau species starting at residues Met11 and Gln124 (accordingly to the longest Tau isoform) regarding Tau microtubule function. Our results surprisingly showed that the ability of Tau to bind and stabilize microtubules was greater when the first 123 residues are truncated, suggesting that Tau N-terminus would have a role in regulation of microtubule stabilization. Overall, future studies based on our new N-terminally truncated-Tau species will provide new knowledge on the role of truncation in Tau biology as well as in AD pathological process.
HostingRepository	PRIDE
AnnounceDate	2015-05-15
AnnouncementXML	Submission_2015-05-18_04:06:56.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD001353
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Yann Verdier
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue; acetylated residue; dehydrated residue; iodoacetamide derivatized residue; thioacylation of primary amines - site K; deaminated residue; thioacylation of primary amines - site N-term
Instrument	LTQ FT

Revision	Datetime	Status	ChangeLog Entry
0	2014-09-22 03:25:05	ID requested
1	2015-05-15 08:58:43	announced
⏵ 2	2015-05-18 04:06:58	announced	Updated publication reference for PubMed record(s): 25974414.

Derisbourg M, Leghay C, Chiappetta G, Fernandez-Gomez FJ, Laurent C, Demeyer D, Carrier S, Bu, é, e-Scherrer V, Blum D, Vinh J, Sergeant N, Verdier Y, Bu, é, e L, Hamdane M, Role of the Tau N-terminal region in microtubule stabilization revealed by new endogenous truncated forms. Sci Rep, 5():9659(2015) [pubmed]

curator keyword: Biomedical

submitter keyword: Tau

Alzheimer's disease

Human

LC MS/MS

Joelle VINH
contact affiliation	USR3149 CNRS - ESPCI ParisTech
contact email	joelle.vinh@espci.fr
lab head
Yann Verdier
contact affiliation	SMBP
contact email	yann.verdier@espci.fr
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/2015/05/PXD001353

PRIDE project URI

• PRIDE
  1. PXD001353
     1. Label: PRIDE project
     2. Name: Truncated Tau