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Journal article

Structural and biochemical characterization of the KLHL3-WNK kinase interaction important in blood pressure regulation.

Abstract:

WNK1 [with no lysine (K)] and WNK4 regulate blood pressure by controlling the activity of ion co-transporters in the kidney. Groundbreaking work has revealed that the ubiquitylation and hence levels of WNK isoforms are controlled by a Cullin-RING E3 ubiquitin ligase complex (CRL3KLHL3) that utilizes CUL3 (Cullin3) and its substrate adaptor, KLHL3 (Kelch-like protein 3). Loss-of-function mutations in either CUL3 or KLHL3 cause the hereditary high blood pressure disease Gordon's syndrome by sta...

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Publication status:
Published

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Publisher copy:
10.1042/bj20140153

Authors


Schumacher, FR More by this author
Sorrell, FJ More by this author
Alessi, DR More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Publisher:
Portland Press Ltd
Journal:
The Biochemical journal
Volume:
460
Issue:
2
Pages:
237-246
Publication date:
2014-06-05
DOI:
EISSN:
1470-8728
ISSN:
0264-6021
URN:
uuid:1938bfce-99ae-465e-bbaa-038574426f4a
Source identifiers:
457860
Local pid:
pubs:457860

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