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Journal article

Sequence and structural variations determining the recruitment of WNK kinases to the KLHL3 E3 ligase

Abstract:

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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Publisher copy:
10.1042/bcj20220019

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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:
0264-6021
Pmid:
35179207
Language:
English
Keywords:
Pubs id:
1240783
Local pid:
pubs:1240783
Deposit date:
2022-02-23

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