{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Okamoto K"],"funding":["NCPDCID CDC HHS","NINDS NIH HHS"],"pagination":["9608-20"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1265801"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["25(21)"],"pubmed_abstract":["Understanding how p53 activity is regulated is crucial in elucidating mechanisms of cellular defense against cancer. Genetic data indicate that Mdmx as well as Mdm2 plays a major role in maintaining p53 activity at low levels in nonstressed cells. However, biochemical mechanisms of how Mdmx regulates p53 activity are not well understood. Through identification of Mdmx-binding proteins, we found that 14-3-3 proteins are associated with Mdmx. Mdmx harbors a consensus sequence for binding of 14-3-3. Serine 367 (S367) is located within the putative binding sequence for 14-3-3, and its substitution with alanine (S367A) abolishes binding of Mdmx to 14-3-3. Transfection assays indicated that the S367A mutation, in cooperation with Mdm2, enhances the ability of Mdmx to repress the transcriptional "],"journal":["Molecular and cellular biology"],"pubmed_title":["DNA damage-induced phosphorylation of MdmX at serine 367 activates p53 by targeting MdmX for Mdm2-dependent degradation."],"pmcid":["PMC1265801"],"funding_grant_id":["NS 31763","R01 NS031763","NCI 87497"],"pubmed_authors":["Kashima K","Teunisse A","Marine JC","Nota A","Ishida M","Okamoto K","Migliorini D","Jochemsen AG","Taya Y","Shiloh Y","Pereg Y","Kitabayashi I","Yamazaki S","Prives C"],"additional_accession":[]},"is_claimable":false,"name":"DNA damage-induced phosphorylation of MdmX at serine 367 activates p53 by targeting MdmX for Mdm2-dependent degradation.","description":"Understanding how p53 activity is regulated is crucial in elucidating mechanisms of cellular defense against cancer. Genetic data indicate that Mdmx as well as Mdm2 plays a major role in maintaining p53 activity at low levels in nonstressed cells. However, biochemical mechanisms of how Mdmx regulates p53 activity are not well understood. Through identification of Mdmx-binding proteins, we found that 14-3-3 proteins are associated with Mdmx. Mdmx harbors a consensus sequence for binding of 14-3-3. Serine 367 (S367) is located within the putative binding sequence for 14-3-3, and its substitution with alanine (S367A) abolishes binding of Mdmx to 14-3-3. Transfection assays indicated that the S367A mutation, in cooperation with Mdm2, enhances the ability of Mdmx to repress the transcriptional ","dates":{"release":"2005-01-01T00:00:00Z","publication":"2005 Nov","modification":"2025-04-18T16:09:35.155Z","creation":"2019-03-27T01:25:22Z"},"accession":"S-EPMC1265801","cross_references":{"pubmed":["16227609"],"doi":["10.1128/MCB.25.21.9608-9620.2005","10.1128/mcb.25.21.9608-9620.2005"]}}