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- Hearn, Jeff, et al.
(författare)
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Configurations of Europe
- 2006
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Ingår i: European Perspectives on Men and Masculinities. National and Transnational Approaches. - Houndmills, Basingstoke and New York : Palgrave macmillan. - 1403918139 ; , s. 184-199
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Bokkapitel (refereegranskat)
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- Hearn, Jeff, et al.
(författare)
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Home and Work
- 2006
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Ingår i: European Perspectives on Men and Masculinities. National and Transnational Approaches. - Houndmills, Basingstoke and New York : Palgrave macmillan. - 1403918139
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Bokkapitel (refereegranskat)
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4. |
- Hearn, Jeff, et al.
(författare)
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Home and Work
- 2006
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Ingår i: European Perspectives on Men and Masculinities. - London : Palgrave, London. - 1403918139 ; , s. 115-136
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Bokkapitel (refereegranskat)
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- Li, Yitong, et al.
(författare)
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Coupling to short linear motifs creates versatile PME-1 activities in PP2A holoenzyme demethylation and inhibition
- 2022
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Ingår i: eLIFE. - : eLife Sciences Publications Ltd. - 2050-084X. ; 11
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Tidskriftsartikel (refereegranskat)abstract
- Protein phosphatase 2A (PP2A) holoenzymes target broad substrates by recognizing short motifs via regulatory subunits. PP2A methylesterase 1 (PME-1) is a cancer-promoting enzyme and undergoes methylesterase activation upon binding to the PP2A core enzyme. Here, we showed that PME-1 readily demethylates different families of PP2A holoenzymes and blocks substrate recognition in vitro. The high-resolution cryoelectron microscopy structure of a PP2A-B56 holoenzyme-PME-1 complex reveals that PME-1 disordered regions, including a substrate-mimicking motif, tether to the B56 regulatory subunit at remote sites. They occupy the holoenzyme substratebinding groove and allow large structural shifts in both holoenzyme and PME-1 to enable multipartite contacts at structured cores to activate the methylesterase. B56 interface mutations selectively block PME-1 activity toward PP2A-B56 holoenzymes and affect the methylation of a fraction of total cellular PP2A. The B56 interface mutations allow us to uncover B56-specific PME-1 functions in p53 signaling. Our studies reveal multiple mechanisms of PME-1 in suppressing holoenzyme functions and versatile PME-1 activities derived from coupling substrate-mimicking motifs to dynamic structured cores.
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- Pringle, Keith, et al.
(författare)
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Law and Policy
- 2006
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Ingår i: European Perspectives on Men and Masculinities. - London : Palgrave, London. - 1403918139 ; , s. 74-95
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Bokkapitel (refereegranskat)
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