Pentameric Assembly of Potassium Channel Tetramerization Domain-Containing Protein 5
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We report the X-ray crystal structure of human potassium channel tetramerization domain-containing protein 5 (KCTD5), the first member of the family to be so characterized. Four findings were unexpected. First, the structure reveals assemblies of five subunits while tetramers were anticipated; pentameric stoichiometry is observed also in solution by scanning transmission electron microscopy mass analysis and analytical ultracentrifugation. Second, the same BTB (bric-a-brac, tramtrack, broad complex) domain surface mediates the assembly of five KCTD5 and four voltage-gated K(+) (Kv) channel subunits; four amino acid differences appear crucial. Third, KCTD5 complexes have well-defined N- and C-terminal modules separated by a flexible linker that swivels by approximately 30 degrees; the C-module shows a new fold and is required to bind Golgi reassembly stacking protein 55 with approximately 1 microM affinity, as judged by surface plasmon resonance and ultracentrifugation. Fourth, despite the homology reflected in its name, KCTD5 does not impact the operation of Kv4.2, Kv3.4, Kv2.1, or Kv1.2 channels.
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KCTD5 regulates GPCR signalling through ubiquitin-mediated degradation of Gβγ subunits.
“KCTD5, which regulates GPCR signalling through ubiquitin-mediated degradation of Gβγ subunits 85,86 .”
From Targeted protein degradation: expanding the toolbox (2019) · cites this paper as [86]
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A Comprehensive Analysis of the Structural Recognition between KCTD Proteins and Cullin 3
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KCTD5 is endowed with large, functionally relevant, interdomain motions
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KCTD5 and Ubiquitin Proteasome Signaling Are Required for Helicobacter pylori Adherence
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Heterozygous Kctd5 knockout mice exhibit abnormal lipid metabolism
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- Authors
- Dementieva, I. S., Tereshko, V., McCrossan, Z. A., Solomaha, E., Araki, D., Xu, C., Grigorieff, N., & Goldstein, S. A. N.
- Affiliations
- University of Chicago (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Goldstein, Steve A.N.
- ORCID
- Grigorieff, Nikolaus
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2009-03
- Volume
- 387
- Issue
- 1
- Pages
- 175-191
- ISSN
- 0022-2836 (ISSN-L)
- PMC
- PMC2670943
- OpenAlex
- W2034269043
- Cited by
- 79
- References
- 44
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 6 · 2023: 4 · 2022: 2 · 2021: 4 · 2020: 4 · 2019: 7 · 2017: 4 · 2016: 4 · 2015: 6 · 2014: 4 · 2013: 8 · 2012: 10
- FWCI
- 2.55
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- Funders
- National Cancer Institute (Y1-CO-1020)
- National Institute of General Medical Sciences (R01GM051851, Y1-GM-1104)
- National Institute of Neurological Disorders and Stroke (R01NS058505)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- KCTD5, pentameric assembly, BTB domain, protein crystal structure, Kv4.2, Kv3.4, Kv2.1, Kv1.2, voltage-gated potassium channels, protein stoichiometry
- MeSH terms
- Amino Acid Sequence, Biopolymers, Humans, Models, Molecular, Molecular Sequence Data, Protein Conformation, Potassium Channels, Sequence Homology, Amino Acid, Crystallography, X-Ray, Surface Plasmon Resonance, Static Electricity
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