PXD005537

PXD005537 is an original dataset announced via ProteomeXchange.

Title	Proteomics profiling of Neuronal Mitochondria
Description	Mitochondria are the ‘power-houses’ of all cells, generating ATP to fuel numerous pathways which are vital for cellular form and function (1). Neuronal processes and synapses present a constant demand for ATP to maintain ionic gradients and neurotransmission events (2), promoting sub-populations of mitochondria to be enriched pre- and post-synaptically (3, 4). These mitochondria display unique enzymatic (5), calcium buffering (6, 7) and antioxidant properties (8) and have thus been associated in the pathogenesis of a variety of neurodegenerative diseases where the synapse is the primary target. In this study, we employed label-free proteomics to characterize the proteomes of synaptic and non-synaptic mitochondria following biochemical isolation (5). Discrete proteomic profiles exist between the two subpopulations of mitochondria and a molecular fingerprint of these differences is seemingly conserved between mammalian species. The majority of the constituents of this grouping have been previously associated with diseases of the nervous system. In addition, bioinformatic analysis of this conserved expression pattern indicated that differences in the properties of protein complex I may represent an important specialisation of synaptic mitochondria. Following this, in vivo assays of mitochondrial candidates using Drosophila larval fillet preparations were performed. Our data demonstrates that selective knock-down of intrinsic mitochondrial proteins alter synaptic morphology which may contribute to pathological processes during ageing and disease.
HostingRepository	PRIDE
AnnounceDate	2018-10-26
AnnouncementXML	Submission_2018-10-26_12:19:37.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Douglas Lamont
SpeciesList	scientific name: Rattus norvegicus (Rat); NCBI TaxID: 10116;
ModificationList	dihydroxylated residue; 2-pyrrolidone-5-carboxylic acid (Gln); phosphorylated residue; monohydroxylated residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2016-12-09 07:12:34	ID requested
⏵ 1	2018-10-26 12:19:39	announced

Graham LC, Eaton SL, Brunton PJ, Atrih A, Smith C, Lamont DJ, Gillingwater TH, Pennetta G, Skehel P, Wishart TM, Proteomic profiling of neuronal mitochondria reveals modulators of synaptic architecture. Mol Neurodegener, 12(1):77(2017) [pubmed]

curator keyword: Biological

submitter keyword: synapse, mitochondria, proteomics, neuron, neurodegeneration

Tom Wishart
contact affiliation	Division of Neurobiology The Roslin Institute Royal (Dick) School of Veterinary Studies College of Medicine and Veterinary Medicine University of Edinburgh Easter Bush Midlothian EH25 9RG SCOTLAND, UK
contact email	T.M.Wishart@ed.ac.uk
lab head
Douglas Lamont
contact affiliation	School of Life Sciences
contact email	d.j.lamont@dundee.ac.uk
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/2018/10/PXD005537

PRIDE project URI

• PRIDE
  1. PXD005537
     1. Label: PRIDE project
     2. Name: Proteomics profiling of Neuronal Mitochondria