Journal article
Sequence and structural variations determining the recruitment of WNK kinases to the KLHL3 E3 ligase
- Abstract:
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The BTB-Kelch protein KLHL3 is a Cullin3-dependent E3 ligase that mediates the ubiquitin-dependent degradation of kinases WNK1–4 to control blood pressure and cell volume. A crystal structure of KLHL3 has defined its binding to an acidic degron motif containing a PXXP sequence that is strictly conserved in WNK1, WNK2 and WNK4. Mutations in the second proline abrograte the interaction causing the hypertension syndrome pseudohypoaldosteronism type II. WNK3 shows a diverged degron motif containi...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Version of record, 7.4MB)
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- Publisher copy:
- 10.1042/bcj20220019
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Authors
Funding
Bibliographic Details
- Publisher:
- Biochemical Society Publisher's website
- Journal:
- Biochemical Journal Journal website
- Volume:
- 479
- Issue:
- 5
- Pages:
- 661–675
- Publication date:
- 2022-02-18
- Acceptance date:
- 2022-02-18
- DOI:
- EISSN:
-
1470-8728
- ISSN:
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0264-6021
- Pmid:
-
35179207
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
1240783
- Local pid:
- pubs:1240783
- Deposit date:
- 2022-02-23
Terms of use
- Copyright holder:
- Chen et al.
- Copyright date:
- 2022
- Rights statement:
- ©2022 The Author(s). This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY).
- Licence:
- CC Attribution (CC BY)
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