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Sebastian Alers

Researcher at University of Tübingen

Publications -  13
Citations -  2042

Sebastian Alers is an academic researcher from University of Tübingen. The author has contributed to research in topics: Autophagy & Autophagy-related protein 13. The author has an hindex of 11, co-authored 13 publications receiving 1761 citations. Previous affiliations of Sebastian Alers include University of Göttingen.

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Journal ArticleDOI

Role of AMPK-mTOR-Ulk1/2 in the regulation of autophagy: cross talk, shortcuts, and feedbacks.

TL;DR: This review focuses on the serine/threonine protein kinases AMP-activated protein kinase, mammalian target of rapamycin (mTOR), and unc-51-like kinase 1/2 (Ulk1/2), three interconnected major junctions within the autophagy regulating signaling network.
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Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop

TL;DR: It is reported that Ulk1/2 in turn phosphorylates all three subunits of AMPK and thereby negatively regulates its activity and is proposed thatUlk1 is not only involved in the induction of autophagy, but also in terminating signaling events that trigger autophagic induction.
Journal ArticleDOI

AMPK-independent induction of autophagy by cytosolic Ca2+ increase.

TL;DR: It is suggested that apart from reported AM PK-dependent regulation of autophagic degradation, an AMPK-independent pathway triggers Ca(2+)-mediated autophagy, involving the PI(3)P-effector protein WIPI-1 and LC3.
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Atg13 and FIP200 act independently of Ulk1 and Ulk2 in autophagy induction

TL;DR: In this paper, Atg13 has been shown to be indispensable for autophagy induction in Atg-deficient cells, and the simultaneous knockout of Ulk1 and Ulk2 did not have a similar effect on autophagia induction.

2011 Landes Bioscience. Do not distribute. Atg13 and FIP200 act independently of Ulk1 and Ulk2 in autophagy induction

TL;DR: Atg13 has an additional function independent of Ulk1/2 and that Atg13 and FIP200 act in concert during autophagy induction, and the Ulk 1-dependent phosphorylation sites identified in AtG13 are expendable for this process.