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Coupling to short l...
Coupling to short linear motifs creates versatile PME-1 activities in PP2A holoenzyme demethylation and inhibition
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- Li, Yitong (författare)
- Univ Wisconsin, McArdle Lab Canc Res, Dept Oncol, Sch Med & Publ Hlth, 1400 Univ Ave, Madison, WI 53706 USA.
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- Balakrishnan, Vijaya Kumar (författare)
- Univ Wisconsin, McArdle Lab Canc Res, Dept Oncol, Sch Med & Publ Hlth, 1400 Univ Ave, Madison, WI 53706 USA.
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- Rowse, Michael (författare)
- Univ Wisconsin, McArdle Lab Canc Res, Dept Oncol, Sch Med & Publ Hlth, 1400 Univ Ave, Madison, WI 53706 USA.
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- Wu, Cheng-Guo (författare)
- Univ Wisconsin, McArdle Lab Canc Res, Dept Oncol, Sch Med & Publ Hlth, 1400 Univ Ave, Madison, WI 53706 USA.;Univ Wisconsin, Biophys Program, Madison, WI 53706 USA.
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- Bravos, Anastasia Phoebe (författare)
- Univ Wisconsin, McArdle Lab Canc Res, Dept Oncol, Sch Med & Publ Hlth, 1400 Univ Ave, Madison, WI 53706 USA.
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- Yadav, Vikash K. (författare)
- Uppsala universitet,Institutionen för kemi - BMC
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- Ivarsson, Ylva (författare)
- Uppsala universitet,Biokemi
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- Strack, Stefan (författare)
- Univ Iowa, Dept Neurosci & Pharmacol, Iowa City, IA USA.
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- Novikova, Irina, V (författare)
- Pacific Northwest Natl Lab, Environm Mol Sci Lab, Richland, WA 99352 USA.
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- Xing, Yongna (författare)
- Univ Wisconsin, McArdle Lab Canc Res, Dept Oncol, Sch Med & Publ Hlth, 1400 Univ Ave, Madison, WI 53706 USA.;Univ Wisconsin, Biophys Program, Madison, WI 53706 USA.
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Univ Wisconsin, McArdle Lab Canc Res, Dept Oncol, Sch Med & Publ Hlth, 1400 Univ Ave, Madison, WI 53706 USA Univ Wisconsin, McArdle Lab Canc Res, Dept Oncol, Sch Med & Publ Hlth, 1400 Univ Ave, Madison, WI 53706 USA.;Univ Wisconsin, Biophys Program, Madison, WI 53706 USA. (creator_code:org_t)
- eLife Sciences Publications Ltd, 2022
- 2022
- Engelska.
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Ingår i: eLIFE. - : eLife Sciences Publications Ltd. - 2050-084X. ; 11
- Relaterad länk:
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https://doi.org/10.7...
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https://uu.diva-port... (primary) (Raw object)
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https://doi.org/10.7...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
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Li, Yitong
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Balakrishnan, Vi ...
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Rowse, Michael
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Wu, Cheng-Guo
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Bravos, Anastasi ...
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Yadav, Vikash K.
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visa fler...
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Ivarsson, Ylva
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Strack, Stefan
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Novikova, Irina, ...
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Xing, Yongna
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