Table reporting the summary of quantified complex members and their regulation. (XLSX 179 kb

Alessandro Ori

Amparo Andrés-Pons

Katarzyna Buczak

Luca Parca

Martin Beck

Murat Iskar

Panagiotis Kastritis

Peer Bork

Stephan Singer

Genome Biology

PubMed

Springer - Publisher Connector

Spatiotemporal variation of mammalian protein complex stoichiometries

Crossref

BACKGROUND: Recent large-scale studies revealed cell-type specific proteomes. However, protein complexes, the basic functional modules of a cell, have been so far mostly considered as static entities with well-defined structures. The co-expression of their members has not been systematically charted at the protein level.RESULTS: We used measurements of protein abundance across 11 cell types and five temporal states to analyze the co-expression and the compositional variations of 182 well-characterized protein complexes. We show that although the abundance of protein complex members is generally co-regulated, a considerable fraction of all investigated protein complexes is subject to stoichiometric changes. Compositional variation is most frequently seen in complexes involved in chromatin regulation and cellular transport, and often involves paralog switching as a mechanism for the regulation of complex stoichiometry. We demonstrate that compositional signatures of variable protein complexes have discriminative power beyond individual cell states and can distinguish cancer cells from healthy ones.CONCLUSIONS: Our work demonstrates that many protein complexes contain variable members that cause distinct stoichometries and functionally fine-tune complexes spatiotemporally. Only a fraction of these compositional variations is mediated by changes in transcription and other mechanisms regulating protein abundance contribute to determine protein complex stoichiometries. Our work highlights the superior power of proteome profiles to study protein complexes and their variants across cell states

Ori, A.

Iskar, M.

Buczak, K.

Kastritis, P.

Parca, L.

Andrés-Pons, A.

Singer, S.

Bork, P.

Beck, M.

MPG.PuRe

Background: Recent large-scale studies revealed cell-type specific proteomes. However, protein complexes, the basic functional modules of a cell, have been so far mostly considered as static entities with well-defined structures. The co-expression of their members has not been systematically charted at the protein level. Results: We used measurements of protein abundance across 11 cell types and five temporal states to analyze the co-expression and the compositional variations of 182 well-characterized protein complexes. We show that although the abundance of protein complex members is generally co-regulated, a considerable fraction of all investigated protein complexes is subject to stoichiometric changes. Compositional variation is most frequently seen in complexes involved in chromatin regulation and cellular transport, and often involves paralog switching as a mechanism for the regulation of complex stoichiometry. We demonstrate that compositional signatures of variable protein complexes have discriminative power beyond individual cell states and can distinguish cancer cells from healthy ones. Conclusions: Our work demonstrates that many protein complexes contain variable members that cause distinct stoichometries and functionally fine-tune complexes spatiotemporally. Only a fraction of these compositional variations is mediated by changes in transcription and other mechanisms regulating protein abundance contribute to determine protein complex stoichiometries. Our work highlights the superior power of proteome profiles to study protein complexes and their variants across cell states

Andres-Pons, A.

MDC Repository

English

BACKGROUND: Recent large-scale studies revealed cell-type specific proteomes. However, protein complexes, the basic functional modules of a cell, have been so far mostly considered as static entities with well-defined structures. The co-expression of their members has not been systematically charted at the protein level. RESULTS: We used measurements of protein abundance across 11 cell types and five temporal states to analyze the co-expression and the compositional variations of 182 well-characterized protein complexes. We show that although the abundance of protein complex members is generally co-regulated, a considerable fraction of all investigated protein complexes is subject to stoichiometric changes. Compositional variation is most frequently seen in complexes involved in chromatin regulation and cellular transport, and often involves paralog switching as a mechanism for the regulation of complex stoichiometry. We demonstrate that compositional signatures of variable protein complexes have discriminative power beyond individual cell states and can distinguish cancer cells from healthy ones. CONCLUSIONS: Our work demonstrates that many protein complexes contain variable members that cause distinct stoichometries and functionally fine-tune complexes spatiotemporally. Only a fraction of these compositional variations is mediated by changes in transcription and other mechanisms regulating protein abundance contribute to determine protein complex stoichiometries. Our work highlights the superior power of proteome profiles to study protein complexes and their variants across cell states

Ori, Alessandro

Iskar, Murat

Buczak, Katarzyna

Kastritis, Panagiotis

Parca, Luca

Andres-Pons, Amparo

Singer, Stephan

Beck, Martin

Hochschulbibliothekszentrum des Landes Nordrhein-Westfalen (hbz)

Table listing the protein complex resource. (XLSX 42 kb

Alessandro Ori (2302189)

Murat Iskar (189860)

Katarzyna Buczak (3404135)

Panagiotis Kastritis (844356)

Luca Parca (116758)

Amparo AndrĂŠs-Pons (3404141)

Stephan Singer (3404138)

Peer Bork (438)

Martin Beck (844357)

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Additional file 2: of Spatiotemporal variation of mammalian protein complex stoichiometries

Additional file 6: of Spatiotemporal variation of mammalian protein complex stoichiometries

http://edoc.mdc-berlin.de/15584/1/15584oa.pdf

Spatiotemporal variation of mammalian protein complex stoichiometries

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MPG.PuRe

MDC Repository

Springer - Publisher Connector

Hochschulbibliothekszentrum des Landes Nordrhein-Westfalen (hbz)

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