CaMKII-mediated Beclin 1 phosphorylation regulates autophagy that promotes degradation of Id and neuroblastoma cell differentiation

Autophagy is a degradative pathway that delivers cellular components to the lysosome for degradation. The role of autophagy in cell differentiation is poorly understood. Here we show that CaMKII can directly phosphorylate Beclin 1 at Ser90 to promote K63-linked ubiquitination of Beclin 1 and activat...

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Published inNature communications Vol. 8; no. 1; pp. 1159 - 16
Main Authors Li, Xuan, Wu, Xiao-Qi, Deng, Rong, Li, Dan-Dan, Tang, Jun, Chen, Wen-Dan, Chen, Jing-Hong, Ji, Jiao, Jiao, Lin, Jiang, Shan, Yang, Fen, Feng, Gong-Kan, Senthilkumar, Ravichandran, Yue, Fei, Zhang, Hai-Liang, Wu, Rui-Yan, Yu, Yan, Xu, Xue-Lian, Mai, Jia, Li, Zhi-Ling, Peng, Xiao-Dan, Huang, Yun, Huang, Xiang, Ma, Ning-Fang, Tao, Qian, Zeng, Yi-Xin, Zhu, Xiao-Feng
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 27.10.2017
Nature Publishing Group
Nature Portfolio
Subjects
631/337/458/1733
631/67/71
631/80/39
Autophagy
Ca2+/calmodulin-dependent protein kinase II
Cell differentiation
Degradation
Differentiation (biology)
Humanities and Social Sciences
multidisciplinary
Neuroblastoma
Neuroblasts
Phagocytosis
Phosphorylation
Proteins
Science
Science (multidisciplinary)
Ubiquitination
Online AccessGet full text
ISSN2041-1723
2041-1723
DOI10.1038/s41467-017-01272-2

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Abstract Autophagy is a degradative pathway that delivers cellular components to the lysosome for degradation. The role of autophagy in cell differentiation is poorly understood. Here we show that CaMKII can directly phosphorylate Beclin 1 at Ser90 to promote K63-linked ubiquitination of Beclin 1 and activation of autophagy. Meanwhile, CaMKII can also promote K63-linked ubiquitination of inhibitor of differentiation 1/2 (Id-1/2) by catalyzing phosphorylation of Id proteins and recruiting TRAF-6. Ubiquitinated Id-1/Id-2 can then bind to p62 and be transported to autolysosomes for degradation. Id degradation promotes the differentiation of neuroblastoma cells and reduces the proportion of stem-like cells. Our study proposes a mechanism by which autophagic degradation of Id proteins can regulate cell differentiation. This suggests that targeting of CaMKII and the regulation of autophagic degradation of Id may be an effective therapeutic strategy to induce cell differentiation in neuroblastoma. Neuroblastoma cell differentiation is regulated by Id proteins. Here, the authors show that CaMKII-mediated phosphorylation of Beclin 1 can activate K63-linked ubiquitination and autophagic degradation of Id proteins uncovering a role for autophagy in cell differentiation.
AbstractList Autophagy is a degradative pathway that delivers cellular components to the lysosome for degradation. The role of autophagy in cell differentiation is poorly understood. Here we show that CaMKII can directly phosphorylate Beclin 1 at Ser90 to promote K63-linked ubiquitination of Beclin 1 and activation of autophagy. Meanwhile, CaMKII can also promote K63-linked ubiquitination of inhibitor of differentiation 1/2 (Id-1/2) by catalyzing phosphorylation of Id proteins and recruiting TRAF-6. Ubiquitinated Id-1/Id-2 can then bind to p62 and be transported to autolysosomes for degradation. Id degradation promotes the differentiation of neuroblastoma cells and reduces the proportion of stem-like cells. Our study proposes a mechanism by which autophagic degradation of Id proteins can regulate cell differentiation. This suggests that targeting of CaMKII and the regulation of autophagic degradation of Id may be an effective therapeutic strategy to induce cell differentiation in neuroblastoma.
Autophagy is a degradative pathway that delivers cellular components to the lysosome for degradation. The role of autophagy in cell differentiation is poorly understood. Here we show that CaMKII can directly phosphorylate Beclin 1 at Ser90 to promote K63-linked ubiquitination of Beclin 1 and activation of autophagy. Meanwhile, CaMKII can also promote K63-linked ubiquitination of inhibitor of differentiation 1/2 (Id-1/2) by catalyzing phosphorylation of Id proteins and recruiting TRAF-6. Ubiquitinated Id-1/Id-2 can then bind to p62 and be transported to autolysosomes for degradation. Id degradation promotes the differentiation of neuroblastoma cells and reduces the proportion of stem-like cells. Our study proposes a mechanism by which autophagic degradation of Id proteins can regulate cell differentiation. This suggests that targeting of CaMKII and the regulation of autophagic degradation of Id may be an effective therapeutic strategy to induce cell differentiation in neuroblastoma. Neuroblastoma cell differentiation is regulated by Id proteins. Here, the authors show that CaMKII-mediated phosphorylation of Beclin 1 can activate K63-linked ubiquitination and autophagic degradation of Id proteins uncovering a role for autophagy in cell differentiation.
Autophagy is a degradative pathway that delivers cellular components to the lysosome for degradation. The role of autophagy in cell differentiation is poorly understood. Here we show that CaMKII can directly phosphorylate Beclin 1 at Ser90 to promote K63-linked ubiquitination of Beclin 1 and activation of autophagy. Meanwhile, CaMKII can also promote K63-linked ubiquitination of inhibitor of differentiation 1/2 (Id-1/2) by catalyzing phosphorylation of Id proteins and recruiting TRAF-6. Ubiquitinated Id-1/Id-2 can then bind to p62 and be transported to autolysosomes for degradation. Id degradation promotes the differentiation of neuroblastoma cells and reduces the proportion of stem-like cells. Our study proposes a mechanism by which autophagic degradation of Id proteins can regulate cell differentiation. This suggests that targeting of CaMKII and the regulation of autophagic degradation of Id may be an effective therapeutic strategy to induce cell differentiation in neuroblastoma.Autophagy is a degradative pathway that delivers cellular components to the lysosome for degradation. The role of autophagy in cell differentiation is poorly understood. Here we show that CaMKII can directly phosphorylate Beclin 1 at Ser90 to promote K63-linked ubiquitination of Beclin 1 and activation of autophagy. Meanwhile, CaMKII can also promote K63-linked ubiquitination of inhibitor of differentiation 1/2 (Id-1/2) by catalyzing phosphorylation of Id proteins and recruiting TRAF-6. Ubiquitinated Id-1/Id-2 can then bind to p62 and be transported to autolysosomes for degradation. Id degradation promotes the differentiation of neuroblastoma cells and reduces the proportion of stem-like cells. Our study proposes a mechanism by which autophagic degradation of Id proteins can regulate cell differentiation. This suggests that targeting of CaMKII and the regulation of autophagic degradation of Id may be an effective therapeutic strategy to induce cell differentiation in neuroblastoma.
Neuroblastoma cell differentiation is regulated by Id proteins. Here, the authors show that CaMKII-mediated phosphorylation of Beclin 1 can activate K63-linked ubiquitination and autophagic degradation of Id proteins uncovering a role for autophagy in cell differentiation.
ArticleNumber 1159
Author Deng, Rong
Tao, Qian
Mai, Jia
Senthilkumar, Ravichandran
Huang, Xiang
Li, Xuan
Jiao, Lin
Wu, Rui-Yan
Wu, Xiao-Qi
Li, Dan-Dan
Tang, Jun
Chen, Wen-Dan
Ji, Jiao
Zhang, Hai-Liang
Feng, Gong-Kan
Zeng, Yi-Xin
Chen, Jing-Hong
Li, Zhi-Ling
Zhu, Xiao-Feng
Peng, Xiao-Dan
Yang, Fen
Ma, Ning-Fang
Jiang, Shan
Yue, Fei
Yu, Yan
Xu, Xue-Lian
Huang, Yun
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/29079782$$D View this record in MEDLINE/PubMed
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Snippet Autophagy is a degradative pathway that delivers cellular components to the lysosome for degradation. The role of autophagy in cell differentiation is poorly...
Neuroblastoma cell differentiation is regulated by Id proteins. Here, the authors show that CaMKII-mediated phosphorylation of Beclin 1 can activate K63-linked...
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SubjectTerms 631/337/458/1733
631/67/71
631/80/39
Autophagy
Ca2+/calmodulin-dependent protein kinase II
Cell differentiation
Degradation
Differentiation (biology)
Humanities and Social Sciences
multidisciplinary
Neuroblastoma
Neuroblasts
Phagocytosis
Phosphorylation
Proteins
Science
Science (multidisciplinary)
Ubiquitination
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Title CaMKII-mediated Beclin 1 phosphorylation regulates autophagy that promotes degradation of Id and neuroblastoma cell differentiation
URI https://link.springer.com/article/10.1038/s41467-017-01272-2
https://www.ncbi.nlm.nih.gov/pubmed/29079782
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https://pubmed.ncbi.nlm.nih.gov/PMC5660092
https://doaj.org/article/efa154aa063f4ab3b297d24aa034cdbf
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