EBSCO Logo
Connecting you to content on EBSCOhost
Results
Title

Interactors and neighbors of ULK1 complex members.

Authors

Sankar, Devanarayanan Siva; Dengjel, Joern

Abstract

The ULK1 kinase complex plays a crucial role in autophagosome biogenesis. To identify interactors or regulators of ULK1 complex assembly influencing autophagosome biogenesis, we performed an interaction proteomics screen. Employing both affinity purification and proximity labeling of N- and C-terminal tagged fusion proteins coupled to quantitative mass spectrometry, we identified 317 high-confidence interactors or neighbors of the four ULK1 complex members, including both member-specific and common interactors. Interactions with selective macroautophagy/autophagy receptors indicate the activation of selective autophagy pathways by 90 min of nutrient starvation. Focusing on the ULK1 effector protein BAG2, a common interactor identified by both approaches, we highlight that ULK1 phosphorylates BAG2, supporting the localization of the scaffold and autophagy inducer AMBRA1 to the ER, thereby positively regulating autophagy initiation. Abbreviation: AMBRA1: autophagy and beclin 1 regulator 1; ATG: autophagy related; ER: endoplasmic reticulum; HA: hemagglutinin; KD: knockdown; KO: knockout; MS: mass spectrometry; PTM: posttranslational modification; RB1CC1/FIP200: RB1 inducible coiled-coil 1; SQSTM1/p62: sequestosome 1; ULK1: unc-51 like autophagy activating kinase 1; WIPI2: WD repeat domain, phosphoinositide interacting 2.

Subjects

ENDOPLASMIC reticulum; CHIMERIC proteins; MASS spectrometry; AUTOPHAGY; PROTEOMICS

Publication

Autophagy, 2025, Vol 21, Issue 1, p243

ISSN

1554-8627

Publication type

Academic Journal

DOI

10.1080/15548627.2024.2414386

EBSCO Connect | Privacy policy | Terms of use | Copyright | Manage my cookies
Journals | Subjects | Sitemap
© 2025 EBSCO Industries, Inc. All rights reserved