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Data · collection · 2015

ATM-mediated PTEN phosphorylation promotes PTEN nuclear translocation and autophagy in response to DNA-damaging agents in cancer cells

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PTEN (phosphatase and tensin homolog), a tumor suppressor frequently mutated in human cancer, has various cytoplasmic and nuclear functions.

Description

PTEN translocates to the nucleus from the cytoplasm in response to oxidative stress. However, the mechanism and function of the translocation are not completely understood.

In this study, topotecan (TPT), a topoisomerase I inhibitor, and cisplatin (CDDP) were employed to induce DNA damage. The results indicate that TPT or CDDP activates ATM (ATM serine/threonine kinase), which phosphorylates PTEN at serine 113 and further regulates PTEN nuclear translocation in A549 and HeLa cells. After nuclear translocation, PTEN induces autophagy, in association with the activation of the p-JUN-SESN2/AMPK pathway, in response to TPT.

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These results identify PTEN phosphorylation by ATM as essential for PTEN nuclear translocation and the subsequent induction of autophagy in response to DNA damage.

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From keywords
Cancer · Cancer
Provenance · 2 source records, 13 field assertions
SourceKeyLast seenRaw
DataCite10.6084/m9.figshare.c.203894915 d agoJSON v1
DataCite10.6084/m9.figshare.c.2038949.v115 d agoJSON v1
FieldAssertionExtractorEvidence
access_levelsource · DataCiteconnector:datacite@1.0.0/data/attributes/rightsList
concepts[disease].local:disease:cancermapping · DataCitevocabulary-mapper@1.0.0keywords['Cancer']
concepts[disease].local:disease:cancermapping · DataCitevocabulary-mapper@1.0.0keywords['Cancer']
concepts[field].fos:biological-sciencessource · DataCiteconnector:datacite@1.0.0
concepts[field].fos:biological-sciencessource · DataCiteconnector:datacite@1.0.0
concepts[field].fos:clinical-medicinesource · DataCiteconnector:datacite@1.0.0
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