File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1016/j.molcel.2021.04.001
- Scopus: eid_2-s2.0-85107013633
- PMID: 33894155
- WOS: WOS:000674490700016
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: A tri-functional amino acid enables mapping of binding sites for posttranslational-modification-mediated protein-protein interactions
Title | A tri-functional amino acid enables mapping of binding sites for posttranslational-modification-mediated protein-protein interactions |
---|---|
Authors | |
Keywords | Protein-protein interactions Histone chaperone Photo-crosslinking Intrinsically disordered domain Posttranslational modification Methylation reader Photoaffinity probes Binding site Proteomics |
Issue Date | 2021 |
Publisher | Cell Press. The Journal's web site is located at http://www.elsevier.com/locate/molcel |
Citation | Molecular Cell, 2021, v. 81 n. 12, p. 2669-2681.e9 How to Cite? |
Abstract | Posttranslational modification (PTM), through the recruitment of effector proteins (i.e., 'readers') that signal downstream events, plays key roles in regulating a variety of cellular processes. To understand how a PTM is recognized, it is necessary to find its readers and, importantly, the location of the binding pockets responsible for PTM recognition. Although various methods have been developed to identify PTM readers, it remains a challenge to directly map the PTM-binding regions, especially for intrinsically disordered domains. Here, we demonstrate a photo-crosslinkable, clickable, and cleavable tri-functional amino acid, ADdis-Cys, that when coupled with mass spectrometry (ADdis-Cys-MS) can not only identify PTM readers from complex proteomes but also simultaneously map their PTM-recognition modules. Using ADdis-Cys-MS, we successfully identify the binding sites of several reader-PTM interactions, among which we discover human C1QBP as a histone chaperone. This robust method should find wide applications in examining other histone or non-histone PTM-mediated protein-protein interactions. |
Persistent Identifier | http://hdl.handle.net/10722/306486 |
ISSN | 2023 Impact Factor: 14.5 2023 SCImago Journal Rankings: 9.332 |
ISI Accession Number ID |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lin, J | - |
dc.contributor.author | Bao, X | - |
dc.contributor.author | Li, XD | - |
dc.date.accessioned | 2021-10-22T07:35:18Z | - |
dc.date.available | 2021-10-22T07:35:18Z | - |
dc.date.issued | 2021 | - |
dc.identifier.citation | Molecular Cell, 2021, v. 81 n. 12, p. 2669-2681.e9 | - |
dc.identifier.issn | 1097-2765 | - |
dc.identifier.uri | http://hdl.handle.net/10722/306486 | - |
dc.description.abstract | Posttranslational modification (PTM), through the recruitment of effector proteins (i.e., 'readers') that signal downstream events, plays key roles in regulating a variety of cellular processes. To understand how a PTM is recognized, it is necessary to find its readers and, importantly, the location of the binding pockets responsible for PTM recognition. Although various methods have been developed to identify PTM readers, it remains a challenge to directly map the PTM-binding regions, especially for intrinsically disordered domains. Here, we demonstrate a photo-crosslinkable, clickable, and cleavable tri-functional amino acid, ADdis-Cys, that when coupled with mass spectrometry (ADdis-Cys-MS) can not only identify PTM readers from complex proteomes but also simultaneously map their PTM-recognition modules. Using ADdis-Cys-MS, we successfully identify the binding sites of several reader-PTM interactions, among which we discover human C1QBP as a histone chaperone. This robust method should find wide applications in examining other histone or non-histone PTM-mediated protein-protein interactions. | - |
dc.language | eng | - |
dc.publisher | Cell Press. The Journal's web site is located at http://www.elsevier.com/locate/molcel | - |
dc.relation.ispartof | Molecular Cell | - |
dc.subject | Protein-protein interactions | - |
dc.subject | Histone chaperone | - |
dc.subject | Photo-crosslinking | - |
dc.subject | Intrinsically disordered domain | - |
dc.subject | Posttranslational modification | - |
dc.subject | Methylation reader | - |
dc.subject | Photoaffinity probes | - |
dc.subject | Binding site | - |
dc.subject | Proteomics | - |
dc.title | A tri-functional amino acid enables mapping of binding sites for posttranslational-modification-mediated protein-protein interactions | - |
dc.type | Article | - |
dc.identifier.email | Lin, J: jlinab@hku.hk | - |
dc.identifier.email | Bao, X: baoxc@hku.hk | - |
dc.identifier.email | Li, XD: xiangli@hku.hk | - |
dc.identifier.authority | Bao, X=rp02881 | - |
dc.identifier.authority | Li, XD=rp01562 | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1016/j.molcel.2021.04.001 | - |
dc.identifier.pmid | 33894155 | - |
dc.identifier.scopus | eid_2-s2.0-85107013633 | - |
dc.identifier.hkuros | 329012 | - |
dc.identifier.volume | 81 | - |
dc.identifier.issue | 12 | - |
dc.identifier.spage | 2669 | - |
dc.identifier.epage | 2681.e9 | - |
dc.identifier.isi | WOS:000674490700016 | - |
dc.publisher.place | United States | - |