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The Incredible ULKs: Autophagy and Beyond | JoVE Visualize

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The Incredible ULKs: Autophagy and Beyond

Yan G Zhao¹, Hong Zhang¹

¹National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China.

Molecular Cell|May 21, 2016

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View abstract on PubMed

Summary

Mammalian Atg1 homologs ULK1/2 are not essential for neuronal basal autophagy. These proteins regulate endoplasmic reticulum export independently of autophagy, revealing new functions for autophagy-related proteins.

Area of Science:

Cell Biology
Molecular Biology
Neuroscience

Background:

Autophagy is a fundamental cellular process regulated by the Atg1 kinase complex.
The Atg1 complex integrates nutrient signals to control autophagy initiation.
The functions of mammalian Atg1 homologs, ULK1 and ULK2, are not fully understood, particularly in neurons.

Purpose of the Study:

To investigate the role of mammalian Atg1 homologs, ULK1 and ULK2, in neuronal basal autophagy.
To explore autophagy-independent functions of ULK1/2 in neuronal cells.

Main Methods:

Utilized knockout mouse models lacking ULK1 and ULK2 in neurons.
Assessed basal autophagy levels using biochemical and imaging techniques.
Investigated the interaction of ULK1/2 with SEC16A and its role in ER export.

Main Results:

Neuronal basal autophagy proceeds normally in mice lacking ULK1 and ULK2.
ULK1/2 were found to phosphorylate SEC16A, a key regulator of ER export.
This phosphorylation event suggests a role for ULK1/2 in regulating ER-associated protein production and secretion, independent of autophagy.

Conclusions:

Mammalian Atg1 homologs ULK1/2 are dispensable for basal autophagy in neurons.
ULK1/2 possess significant autophagy-independent functions, including the regulation of ER export via SEC16A phosphorylation.
These findings expand the known functions of autophagy-related proteins beyond their role in the autophagic pathway.

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The Incredible Ulks: Autophagy And Beyond