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  Characterization of early autophagy signaling by quantitative phosphoproteomics

Rigbolt, K. T. G., Zarei, M., Sprenger, A., Becker, A. C., Diedrich, B., Huang, X., et al. (2014). Characterization of early autophagy signaling by quantitative phosphoproteomics. Autophagy, 10(2), 356-371. doi:10.4161/auto.26864.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-A0F3-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-A0F4-C
Genre: Journal Article

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 Creators:
Rigbolt, Kristoffer T. G., Author
Zarei, Mostafa, Author
Sprenger, Adrian, Author
Becker, Andrea C., Author
Diedrich, Britta, Author
Huang, Xun, Author
Eiselein, Sven, Author
Kristensen, Anders R., Author
Gretzmeier, Christine, Author
Andersen, Jens S., Author
Zi, Zhike1, Author              
Dengjel, Jörn, Author
Affiliations:
1Cell Signaling Dynamics (Zhike Zi), Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_2117284              

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Free keywords: autophagy, signal transduction, phosphorylation, proteomics, phosphoproteomics, mass spectrometry, bioinformatics
 Abstract: Under conditions of nutrient shortage autophagy is the primary cellular mechanism ensuring availability of substrates for continuous biosynthesis. Subjecting cells to starvation or rapamycin efficiently induces autophagy by inhibiting the MTOR signaling pathway triggering increased autophagic flux. To elucidate the regulation of early signaling events upon autophagy induction, we applied quantitative phosphoproteomics characterizing the temporal phosphorylation dynamics after starvation and rapamycin treatment. We obtained a comprehensive atlas of phosphorylation kinetics within the first 30 min upon induction of autophagy with both treatments affecting widely different cellular processes. The identification of dynamic phosphorylation already after 2 min demonstrates that the earliest events in autophagy signaling occur rapidly after induction. The data was subjected to extensive bioinformatics analysis revealing regulated phosphorylation sites on proteins involved in a wide range of cellular processes and an impact of the treatments on the kinome. To approach the potential function of the identified phosphorylation sites we performed a screen for MAP1LC3-interacting proteins and identified a group of binding partners exhibiting dynamic phosphorylation patterns. The data presented here provide a valuable resource on phosphorylation events underlying early autophagy induction.

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Language(s): eng - English
 Dates: 2013-11-212014-02
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.4161/auto.26864
 Degree: -

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Title: Autophagy
Source Genre: Journal
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Publ. Info: Georgetown, TX : Landes Bioscience
Pages: - Volume / Issue: 10 (2) Sequence Number: - Start / End Page: 356 - 371 Identifier: ISSN: 1554-8627
CoNE: /journals/resource/1000000000238500