Structural basis of the heterodimerization of the MST and RASSF SARAH domains in the Hippo signalling pathway
DC Field | Value | Language |
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dc.contributor.author | Hwang, Eunha | - |
dc.contributor.author | Cheong, Hae-Kap | - |
dc.contributor.author | Ul Mushtaq, Ameeq | - |
dc.contributor.author | Kim, Hye-Yeon | - |
dc.contributor.author | Yeo, Kwon Joo | - |
dc.contributor.author | Kim, Eunhee | - |
dc.contributor.author | Lee, Woo Cheol | - |
dc.contributor.author | Hwang, Kwang Yeon | - |
dc.contributor.author | Cheong, Chaejoon | - |
dc.contributor.author | Jeon, Young Ho | - |
dc.date.accessioned | 2021-09-05T07:12:14Z | - |
dc.date.available | 2021-09-05T07:12:14Z | - |
dc.date.created | 2021-06-15 | - |
dc.date.issued | 2014-07 | - |
dc.identifier.issn | 2059-7983 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/98016 | - |
dc.description.abstract | Despite recent progress in research on the Hippo signalling pathway, the structural information available in this area is extremely limited. Intriguingly, the homodimeric and heterodimeric interactions of mammalian sterile 20-like (MST) kinases through the so-called 'SARAH' (SAV/RASSF/HPO) domains play a critical role in cellular homeostasis, dictating the fate of the cell regarding cell proliferation or apoptosis. To understand the mechanism of the heterodimerization of SARAH domains, the three-dimensional structures of an MST1-RASSF5 SARAH heterodimer and an MST2 SARAH homodimer were determined by X-ray crystallography and were analysed together with that previously determined for the MST1 SARAH homodimer. While the structure of the MST2 homodimer resembled that of the MST1 homodimer, the MST1-RASSF5 heterodimer showed distinct structural features. Firstly, the six N-terminal residues (Asp432-Lys437), which correspond to the short N-terminal 310-helix h1 kinked from the h2 helix in the MST1 homodimer, were disordered. Furthermore, the MST1 SARAH domain in the MST1-RASSF5 complex showed a longer helical structure (Ser438-Lys480) than that in the MST1 homodimer (Val441-Lys480). Moreover, extensive polar and nonpolar contacts in the MST1-RASSF5 SARAH domain were identified which strengthen the interactions in the heterodimer in comparison to the interactions in the homodimer. Denaturation experiments performed using urea also indicated that the MST-RASSF heterodimers are substantially more stable than the MST homodimers. These findings provide structural insights into the role of the MST1-RASSF5 SARAH domain in apoptosis signalling. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | INT UNION CRYSTALLOGRAPHY | - |
dc.subject | CELL-PROLIFERATION | - |
dc.subject | PROTEIN-KINASES | - |
dc.subject | GROWTH | - |
dc.subject | MODEL | - |
dc.subject | ASSOCIATION | - |
dc.subject | APOPTOSIS | - |
dc.subject | SALVADOR | - |
dc.subject | CLONING | - |
dc.title | Structural basis of the heterodimerization of the MST and RASSF SARAH domains in the Hippo signalling pathway | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Hwang, Kwang Yeon | - |
dc.contributor.affiliatedAuthor | Jeon, Young Ho | - |
dc.identifier.doi | 10.1107/S139900471400947X | - |
dc.identifier.scopusid | 2-s2.0-84903954341 | - |
dc.identifier.wosid | 000338917000015 | - |
dc.identifier.bibliographicCitation | ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, v.70, pp.1944 - 1953 | - |
dc.relation.isPartOf | ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | - |
dc.citation.title | ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | - |
dc.citation.volume | 70 | - |
dc.citation.startPage | 1944 | - |
dc.citation.endPage | 1953 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Crystallography | - |
dc.relation.journalWebOfScienceCategory | Biochemical Research Methods | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Crystallography | - |
dc.subject.keywordPlus | CELL-PROLIFERATION | - |
dc.subject.keywordPlus | PROTEIN-KINASES | - |
dc.subject.keywordPlus | GROWTH | - |
dc.subject.keywordPlus | MODEL | - |
dc.subject.keywordPlus | ASSOCIATION | - |
dc.subject.keywordPlus | APOPTOSIS | - |
dc.subject.keywordPlus | SALVADOR | - |
dc.subject.keywordPlus | CLONING | - |
dc.subject.keywordAuthor | Hippo signalling pathway | - |
dc.subject.keywordAuthor | MST | - |
dc.subject.keywordAuthor | RASSF | - |
dc.subject.keywordAuthor | SARAH domains | - |
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