Phosphorylation of the pseudokinase Ulk4 by Stk36 promotes primary ciliary tip localization of both proteins to facilitate the phosphorylation and activation of Gli in response to Sonic hedgehog.

ULK3 is a kinase in the abscission checkpoint that temporarily inactivates ESCRT-III proteins via phosphorylation, which is required to delay cytokinesis in response to defects in mitosis.

Quantitative phosphoproteomics defines the substrates for Cyclin A/Cdk1 kinase during early mitosis and follow up studies validate that one identified substrate, MYPT1, influences the stability of k-MT attachments by regulating Plk1.

The control of SEC23B degradation by SCF^FBXW5 and ULK1 regulates the autophagy.

Inhibiting KRAS^G12C and ULK-mediated autophagy is a novel treatment strategy to control the growth of KRAS^G12C-driven lung cancer in preclinical models of lung cancer.

Hydrogen-deuterium exchange, electron microscopy, and vesicle reconstitution show how binding of the autophagy adaptor NDP52 to the FIP200 subunit of the ULK1 complex triggers membrane binding in autophagy.

Using IGF2BP1-PLK1 axis as an example, targeting oncogenic signaling represents a direction treatment for HCC patients with high FBXO45 expression.

An image-based multiplex autophagosome RNAi screen targeting all Rab GTPases as well as their GAPs and GEFs identifies the Rab GEF SMCR8 as multifaceted autophagy modulator, which regulates kinase activity and gene expression of ULK1.

A comprehensive, quantitative, protein-protein interaction screen maps the network of interactions between human MIT domains and ESCRT-III C-terminal tails, and reveals MIT domain-containing protein cofactors for abscission and the 'No Cut' abscission checkpoint.

Pituitary gland size and stem cell number is modulated during early life in the mouse by the imprinted gene Dlk1, which acts in multiple developmental compartments in a dosage-sensitive manner.