File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Phosphorylation-regulated HMGA1a-P53 interaction unveils the function of HMGA1a acidic tail phosphorylations via synthetic proteins

TitlePhosphorylation-regulated HMGA1a-P53 interaction unveils the function of HMGA1a acidic tail phosphorylations via synthetic proteins
Authors
Issue Date2021
PublisherElsevier. The Journal's web site is located at http://www.cell.com/cell-chemical-biology/home
Citation
Cell Chemical Biology, 2021, v. 28 n. 5, p. 722-732.e8 How to Cite?
AbstractAs a typical member of intrinsically disordered proteins (IDPs), HMGA1a carries many post-translational modifications (PTMs). To study the undefined function of acidic tail phosphorylations, seven HMGA1a proteins with site-specific modification(s) were chemically synthesized via Ser/Thr ligation. We found that the phosphorylations significantly inhibit HMGA1a-P53 interaction and the phosphorylations can induce conformational change of HMGA1a from an ‘‘open state’’ to a ‘‘close state.’’ Notably, the positively charged lysinearginine (KR) clusters are responsible for modulating HMGA1a conformation via electrostatic interaction with the phosphorylated acidic tail. Finally, we used a synthetic protein-affinity purification mass spectrometry (SP-AP-MS) methodology to profile the specific interactors, which further supported the function ofHMGA1a phosphorylation. Collectively, this study highlights a mechanism for regulating IDPs’ conformation and function by phosphorylation of non-protein-binding domain and showcases that the protein chemical synthesis in combination with mass spectrometry can serve as an efficient tool to study the IDPs’ PTMs.
Persistent Identifierhttp://hdl.handle.net/10722/300995
ISSN
2023 Impact Factor: 6.6
2023 SCImago Journal Rankings: 2.584
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorWei, T-
dc.contributor.authorliu, H-
dc.contributor.authorchu, B-
dc.contributor.authorBlasco Morales, P-
dc.contributor.authorLiu, Z-
dc.contributor.authorTian, R-
dc.contributor.authorLi, DX-
dc.contributor.authorLi, X-
dc.date.accessioned2021-07-06T03:13:05Z-
dc.date.available2021-07-06T03:13:05Z-
dc.date.issued2021-
dc.identifier.citationCell Chemical Biology, 2021, v. 28 n. 5, p. 722-732.e8-
dc.identifier.issn2451-9456-
dc.identifier.urihttp://hdl.handle.net/10722/300995-
dc.description.abstractAs a typical member of intrinsically disordered proteins (IDPs), HMGA1a carries many post-translational modifications (PTMs). To study the undefined function of acidic tail phosphorylations, seven HMGA1a proteins with site-specific modification(s) were chemically synthesized via Ser/Thr ligation. We found that the phosphorylations significantly inhibit HMGA1a-P53 interaction and the phosphorylations can induce conformational change of HMGA1a from an ‘‘open state’’ to a ‘‘close state.’’ Notably, the positively charged lysinearginine (KR) clusters are responsible for modulating HMGA1a conformation via electrostatic interaction with the phosphorylated acidic tail. Finally, we used a synthetic protein-affinity purification mass spectrometry (SP-AP-MS) methodology to profile the specific interactors, which further supported the function ofHMGA1a phosphorylation. Collectively, this study highlights a mechanism for regulating IDPs’ conformation and function by phosphorylation of non-protein-binding domain and showcases that the protein chemical synthesis in combination with mass spectrometry can serve as an efficient tool to study the IDPs’ PTMs.-
dc.languageeng-
dc.publisherElsevier. The Journal's web site is located at http://www.cell.com/cell-chemical-biology/home-
dc.relation.ispartofCell Chemical Biology-
dc.titlePhosphorylation-regulated HMGA1a-P53 interaction unveils the function of HMGA1a acidic tail phosphorylations via synthetic proteins-
dc.typeArticle-
dc.identifier.emailBlasco Morales, P: pbmoral@hku.hk-
dc.identifier.emailLi, DX: xiangli@hku.hk-
dc.identifier.emailLi, X: xuechenl@hku.hk-
dc.identifier.authorityLi, DX=rp01562-
dc.identifier.authorityLi, X=rp00742-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.chembiol.2021.01.007-
dc.identifier.pmid33545070-
dc.identifier.scopuseid_2-s2.0-85101148714-
dc.identifier.hkuros323091-
dc.identifier.volume28-
dc.identifier.issue5-
dc.identifier.spage722-
dc.identifier.epage732.e8-
dc.identifier.isiWOS:000654307600014-
dc.publisher.placeNetherlands-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats