Atg1 kinase in fission yeast is activated by Atg11-mediated dimerization and cis-autophosphorylation (Q99254866)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:32909946%20AND%20SRC:MED&resulttype=core&format=json

13 September 2020

title

Atg1 kinase in fission yeast is activated by Atg11-mediated dimerization and cis-autophosphorylation (English)

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13 September 2020

1

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13 September 2020

Xiao-Man Liu

3

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13 September 2020

Meng-Qiu Dong

5

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13 September 2020

Li-Lin Du

6

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13 September 2020

author name string

Guang-Can Shao

2

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13 September 2020

Quan Chen

4

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13 September 2020

publication date

10 September 2020

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13 September 2020

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13 September 2020

volume

9

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Autophagy induction under carbon starvation conditions is negatively regulated by carbon catabolite repression.

13 September 2020

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An Atg13 protein-mediated self-association of the Atg1 protein kinase is important for the induction of autophagy

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Atg38-Atg8 interaction in fission yeast establishes a positive feedback loop to promote autophagy

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Early steps in autophagy depend on direct phosphorylation of Atg9 by the Atg1 kinase.

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Kinase domain dimerization drives RIPK3-dependent necroptosis

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How Do Protein Kinases Take a Selfie (Autophosphorylate)?

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FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells

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Activation of protein kinase PKR requires dimerization-induced cis-phosphorylation within the activation loop

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Coomassie staining as loading control in Western blot analysis.

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Regulation of Autophagy By Signaling Through the Atg1/ULK1 Complex

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Identifiers

DOI

10.7554/ELIFE.58073

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:32909946%20AND%20SRC:MED&resulttype=core&format=json

13 September 2020

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