The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Sumoylation Silences the Plasma Membrane Leak K+ Channel K2P1
Open accessAbstract
Reversible, covalent modification with small ubiquitin-related modifier proteins (SUMOs) is known to mediate nuclear import/export and activity of transcription factors. Here, the SUMO pathway is shown to operate at the plasma membrane to control ion channel function. SUMO-conjugating enzyme is seen to be resident in plasma membrane, to assemble with K2P1, and to modify K2P1 lysine 274. K2P1 had not previously shown function despite mRNA expression in heart, brain, and kidney and sequence features like other two-P loop K+ leak (K2P) pores that control activity of excitable cells. Removal of the peptide adduct by SUMO protease reveals K2P1 to be a K+-selective, pH-sensitive, openly rectifying channel regulated by reversible peptide linkage.
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Sumo, ubiquitin's mysterious cousin
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SUMO-1 Conjugation in Vivo Requires Both a Consensus Modification Motif and Nuclear Targeting
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Potassium leak channels and the KCNK family of two-p-domain subunits
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Dai, X.-Q., Plummer, G., Casimir, M., Kang, Y., Hajmrle, C., Gaisano, H. Y., Manning Fox, J. E., & MacDonald, P. E. (2011) · Diabetes · doi:10.2337/db10-0440 · Cited by 92
The function of SUMOylation and its crucial roles in the development of neurological diseases
Chen, X., Zhang, Y., Wang, Q., Qin, Y., Yang, X., Xing, Z., Shen, Y., Wu, H., & Qi, Y. (2021) · The FASEB Journal · doi:10.1096/fj.202002702r · Cited by 39
SUMOylation regulates the homologous to E6-AP carboxyl terminus (HECT) ubiquitin ligase Rsp5p
Novoselova, T. V., Rose, R.-S., Marks, H. M., & Sullivan, J. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.424234 · Cited by 9
Metadata
- Authors
- Rajan, S., Plant, L. D., Rabin, M. L., Butler, M. H., & Goldstein, S. A. N.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2005-04
- Volume
- 121
- Issue
- 1
- Pages
- 37-47
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2076983776
- Cited by
- 263
- References
- 42
- FWCI
- 7.03
- Type
- journal article
- Language
- en
- Open access
- bronze
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
