Dataset Information

PDGF-hSyn Synaptosomes (vGlut FASS) nanoLC-MS/MS

ABSTRACT: This project studies the differential abundance of proteins at excitatory synapses of PDGF-hSyn mice (Masliah et al., 2000, Science), which are a model for Parkinson’s disease/dementia with Lewy bodies. The mice overexpress human alpha synuclein under the human PDGF promoter. Synapses were purified from animals expressing fluorescently tagged vGlut1 (vGlut1-Venus) using fluorescence activated synapse sorting (FASS; cf. Biesemann et al., 2014, EMBO J).

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Mario Dorostkar

LAB HEAD: Mario Dorostkar

PROVIDER: PXD006812 | Pride | 2019-09-02

REPOSITORIES: Pride

ACCESS DATA

Publications

Early defects in translation elongation factor 1α levels at excitatory synapses in α-synucleinopathy.

Blumenstock Sonja S Angelo Maria Florencia MF Peters Finn F Dorostkar Mario M MM Ruf Viktoria C VC Luckner Manja M Crux Sophie S Slapakova Lenka L Arzberger Thomas T Claverol Stéphane S Herzog Etienne E Herms Jochen J

Acta neuropathologica 20190826 6

Cognitive decline and dementia in neurodegenerative diseases are associated with synapse dysfunction and loss, which may precede neuron loss by several years. While misfolded and aggregated α-synuclein is recognized in the disease progression of synucleinopathies, the nature of glutamatergic synapse dysfunction and loss remains incompletely understood. Using fluorescence-activated synaptosome sorting (FASS), we enriched excitatory glutamatergic synaptosomes from mice overexpressing human alpha-s ...[more]

PMID: 31451907

Similar Datasets

Project description:Sturgeons, producers of black caviar, are one of the most valuable wildlife commodities on earth (Pikitch et al., 2005). They appeared approximately 200 million years ago, and are known as living fossils (Bemis et al., 1997). Sturgeon populations dramatically declined as a result of overfishing, poaching and habitat destruction (Birstein, 1993; Billard and Lecointre, 2001; Vidotto et al., 2013). International Union for Conservation of Nature and Natural Resources (IUCN) classified over 85% of sturgeon species as at risk of extinction, more than any other group of species. Therefore, artificial reproduction techniques have been developed for sturgeons to meet the demands of aquaculture and restocking programs. Basic knowledge regarding biology of reproduction such as egg activation and fertilization can help improving the efficiency of artificial reproduction. Fertilization happens when gametes, spermatozoon and egg, are fused together. Egg activation refers to a series of morphological and molecular changes that occur in the egg during and after fertilization. Egg activation is believed to prevent polyspermy, and may also establish a micro-environment to support embryo development (Wong and Wessel, 2006; Niksirat et al., 2015a). Although, earlier researchers have illustrated egg structure and its morphological changes during egg fertilization and activation in sturgeons (Cherr and Clark, 1982, 1985a; Linhart and Kudo, 1997; Debus et al., 2008; Zelazowska, 2010), there is still a lack of molecular knowledge to improve our understanding of this stage of reproduction in these animals. Eggs of sturgeon are released to aqueous environment, where they are fertilized, activated and develop an adhesive layer after contact with freshwater (Cherr and Clark, 1984; Vorobeva and Markov, 1999). Although, egg stickiness is necessary for eggs in nature to help them find a stable position by attaching to substrates such as gravel and stone and increase chance of survival until hatching (Riehl and Patzner, 1998), but can cause high rate of mortality during artificial incubation as a result of attachment of eggs together and subsequent suffocation in limited space of incubators. Using clay suspension in water as an activation medium has been proven to be effective to block egg stickiness in sturgeon eggs (Dettlaff et al., 1993). In recent years, label-free protein quantification techniques have been developed based on the presumption of linear proportionality between peptide mass peak signal intensity and concentration of a given peptide. This approach avoids the limitations and multiple preparation steps of methods such as those based on two-dimensional gel electrophoresis (Niksirat et al., 2015b). The aim of present study was to identify and quantify proteome changes of sterlet eggs during activation in different activation media, water and clay suspension, using label-free protein quantification technique.

Project description:Aluminum (Al) toxicity and phosphate (Pi) limitation are widespread chronic abiotic and mutually enhancing stresses that profoundly affect crop yield. Both stresses causes a strong inhibition of root growth due to a progressive exhaustion of the stem cell niche. Here we report on a CASEIN KINASE 2 (CK2) inhibitor identified by its capability to maintain a functional root stem cell niche under Al toxic conditions. CK2 operates through phosphorylation of the cell cycle checkpoint activator SUPPRESSOR OF GAMMA RADIATION 1 (SOG1), priming its activity under DNA damaging conditions. In addition to yielding Al tolerance, both CK2 and SOG1 inactivation result in resistance to phosphate starvation, revealing the existence of a low phosphate induced cell cycle checkpoint that depends on the DNA damage activator ATAXIA-TELANGIECTASIA MUTATED (ATM). Overall, our data reveal an important physiological role for the plant DNA damage response pathway under agricultural limiting growth conditions and opening new avenues to cope with the problem of Pi limitation. SOG1 can be phosphorylated by both ATM and ATR (Sjogren et al., 2015; Yoshiyama et al., 2017). ATM phosphorylation of SOG1 can occur at five different S/TQ sites upon treatment with double-stand break inducing compounds such as zeocin. This phosphorylation is important for its activity, as demonstrated by the inability of a phosphor-mutant allele to complement the sog1 mutant. In addition to the ATM/ATR-dependent phosphorylation sites, 11 putative CK2 phosphorylation sites [T/SXXE/D, with S or T serving as the phospho-acceptor site (Meggio and Pinna, 2003)] are found within the full length SOG1 proteins. Among these, four sites are conserved among orthologous proteins, stressing their potential importance to protein function. Of these, three cluster at the extreme C-terminus of SOG1, which also is also the location of the ATM/ATR phosphorylation sites. To test putative phosphorylation of any of these sites, TAP-tagged SOG1 protein was extracted and purified from cell cultures and subjected to phosphorylation analysis.

Dataset Information

PDGF-hSyn Synaptosomes (vGlut FASS) nanoLC-MS/MS

Publications

Early defects in translation elongation factor 1α levels at excitatory synapses in α-synucleinopathy.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure