The Incredible ULKs: Autophagy and Beyond
Atg1 integrates nutrient status and autophagy. In this issue, Joo et al. (2016) reveal that the mammalian Atg1 homologs ULK1/2 are dispensable for neuronal basal autophagy. ULK1/2 phosphorylate SEC16A and regulate ER export, expanding the autophagy-independent functions of autophagy proteins. Atg1 i...
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| Published in | Molecular cell Vol. 62; no. 4; pp. 475 - 476 |
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| Abstract | Atg1 integrates nutrient status and autophagy. In this issue, Joo et al. (2016) reveal that the mammalian Atg1 homologs ULK1/2 are dispensable for neuronal basal autophagy. ULK1/2 phosphorylate SEC16A and regulate ER export, expanding the autophagy-independent functions of autophagy proteins.
Atg1 integrates nutrient status and autophagy. In this issue, Joo et al. (2016) reveal that the mammalian Atg1 homologs ULK1/2 are dispensable for neuronal basal autophagy. ULK1/2 phosphorylate SEC16A and regulate ER export, expanding the autophagy-independent functions of autophagy proteins. |
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| AbstractList | Atg1 integrates nutrient status and autophagy. In this issue, Joo et al. (2016) reveal that the mammalian Atg1 homologs ULK1/2 are dispensable for neuronal basal autophagy. ULK1/2 phosphorylate SEC16A and regulate ER export, expanding the autophagy-independent functions of autophagy proteins. Atg1 integrates nutrient status and autophagy. In this issue, Joo et al. (2016) reveal that the mammalian Atg1 homologs ULK1/2 are dispensable for neuronal basal autophagy. ULK1/2 phosphorylate SEC16A and regulate ER export, expanding the autophagy-independent functions of autophagy proteins.Atg1 integrates nutrient status and autophagy. In this issue, Joo et al. (2016) reveal that the mammalian Atg1 homologs ULK1/2 are dispensable for neuronal basal autophagy. ULK1/2 phosphorylate SEC16A and regulate ER export, expanding the autophagy-independent functions of autophagy proteins. Atg1 integrates nutrient status and autophagy. In this issue, Joo et al. (2016) reveal that the mammalian Atg1 homologs ULK1/2 are dispensable for neuronal basal autophagy. ULK1/2 phosphorylate SEC16A and regulate ER export, expanding the autophagy-independent functions of autophagy proteins. Atg1 integrates nutrient status and autophagy. In this issue, Joo et al. (2016) reveal that the mammalian Atg1 homologs ULK1/2 are dispensable for neuronal basal autophagy. ULK1/2 phosphorylate SEC16A and regulate ER export, expanding the autophagy-independent functions of autophagy proteins. Atg1 integrates nutrient status and autophagy. In this issue, Joo et al. (2016) reveal that the mammalian Atg1 homologs ULK1/2 are dispensable for neuronal basal autophagy. ULK1/2 phosphorylate SEC16A and regulate ER export, expanding the autophagy-independent functions of autophagy proteins. |
| Author | Zhang, Hong Zhao, Yan G. |
| Author_xml | – sequence: 1 givenname: Yan G. surname: Zhao fullname: Zhao, Yan G. organization: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China – sequence: 2 givenname: Hong surname: Zhang fullname: Zhang, Hong email: hongzhang@sun5.ibp.ac.cn organization: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, P.R. China |
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| Cites_doi | 10.1038/cr.2013.166 10.1016/j.molcel.2016.04.020 10.1083/jcb.201211014 10.1038/emboj.2011.253 10.1038/ncb2390 10.1038/cr.2013.168 10.1016/j.tcb.2015.03.001 10.1083/jcb.200912082 10.1016/j.cell.2011.10.026 10.1038/cr.2013.159 |
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| SubjectTerms | Animals Autophagy Autophagy-Related Protein-1 Homolog Humans Mammals neurons proteins |
| Title | The Incredible ULKs: Autophagy and Beyond |
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