Organelle proteomics: looking at less to see more

Brunet, Sylvain; Thibault, Pierre; Gagnon, Étienne; Kearney, Paul; Bergeron, John J.M.; Desjardins, Michel

doi:10.1016/j.tcb.2003.10.006

Cited by 159 publications

(99 citation statements)

References 71 publications

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“…Studies using organellar proteomics can reveal proteins that are otherwise masked during whole cell analyses and provide information on protein localization and function, an especially useful tool for studying a virus that usurps many cellular machineries (Brunet et al, 2003;Gilchrist et al, 2006). This work extends our previous finding that HIV-1 replication imposes a blockade to the nuclear import of heterogeneous nuclear RNP A1 (hnRNP A1) and its transport receptor Transportin-1 via alterations in the localization and abundance of Nup p62 (Nup62; Monette et al, 2009).…”

Section: Introductionsupporting

confidence: 62%

HIV-1 remodels the nuclear pore complex

Monette¹,

Panté²,

Mouland³

2011

J Exp Med

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Section: Introductionsupporting

confidence: 62%

HIV-1 remodels the nuclear pore complex

Monette¹,

Panté²,

Mouland³

2011

J Exp Med

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“…In a recent proteomic analysis of purified latex bead-containing phagosomes, we identified Ͼ500 proteins on this organelle by mass spectrometry (31,32). This analysis revealed the presence of four of the components of the ␥-secretase complex, viz.…”

Section: Resultsmentioning

confidence: 99%

γ-Secretase Is a Functional Component of Phagosomes

Jutras

Laplante

Boulais

et al. 2005

Journal of Biological Chemistry

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␥-Secretase is a high molecular mass protein complex that catalyzes the intramembrane cleavage of its protein substrates. Two proteins involved in phagocytosis, CD44 and the low density lipoprotein receptor-related protein, are ␥-secretase substrates, suggesting that this complex might regulate some aspects of phagocytosis. Our results indicate that the four components of ␥-secretase, viz. presenilin, nicastrin, APH-1, and PEN-2, are present and enriched on phagosome membranes from both murine macrophages and Drosophila S2 phagocytes. The ␥-secretase components form high molecular mass complexes in lipid microdomains of the phagosome membrane with the topology expected for the functional enzyme. In contrast to the majority of the phagosome proteins studied so far, which appear to associate transiently with this organelle, ␥-secretase resides on newly formed phagosomes and remains associated throughout their maturation into phagolysosomes. Finally, our results indicate that interferon-␥ stimulates ␥-secretase-dependent cleavages on phagosomes and that ␥-secretase activity may be involved in the phagocytic response of macrophages to inflammatory cytokines.

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“…There has been a tendency to focus on subcellular proteomes concerning specific subcellular compartments and macromolecular structures of the cell (1)(2)(3)(4)(5)(6). The separation of the protein mixture into organelles or other multiprotein complex fractions prior to a proteomics analysis can increase the probability of detecting low-copynumber proteins.…”

mentioning

confidence: 99%

“…The separation of the protein mixture into organelles or other multiprotein complex fractions prior to a proteomics analysis can increase the probability of detecting low-copynumber proteins. Subcellular proteome research cannot only provide information about subcellular location of certain proteins and imply their function, but also tell us the whole-protein components of the specific subcellular fractions (organelles or other multiprotein complexes) and then help understand their structures and biological functions (1)(2)(3)(4)(5)(6).…”

mentioning

confidence: 99%

A Comparative Proteomic Strategy for Subcellular Proteome Research

Jiang

Dai

Sheng

et al. 2005

Molecular & Cellular Proteomics

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Subcellular proteomics, as an important step to functional proteomics, has been a focus in proteomic research. However, the co-purification of "contaminating" proteins has been the major problem in all the subcellular proteomic research including all kinds of mitochondrial proteome research. It is often difficult to conclude whether these "contaminants" represent true endogenous partners or artificial associations induced by cell disruption or incomplete purification. To solve such a problem, we applied a high-throughput comparative proteome experimental strategy, ICAT approach performed with two-dimensional LC-MS/MS analysis, coupled with combinational usage of different bioinformatics tools, to study the proteome of rat liver mitochondria prepared with traditional centrifugation (

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Organelle proteomics: looking at less to see more

Cited by 159 publications

References 71 publications

HIV-1 remodels the nuclear pore complex

HIV-1 remodels the nuclear pore complex

γ-Secretase Is a Functional Component of Phagosomes

A Comparative Proteomic Strategy for Subcellular Proteome Research

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