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Both K63 and K48 ubiquitin linkages signal lysosomal degradation of the LDL receptor

Zhang, Li, Xu, Ming, Scotti, Elena, Chen, Zhijian J., Tontonoz, Peter·2013·Journal of Lipid Research
DOI 10.1194/jlr.m035774PMC PMC3653405
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  • The RING domain of IDOL possesses E3 ligase activity, stimulating poly-K63 and poly-K48 ubiquitination of the cytoplasmic tail of LDLR, thereby marking it for lysosomal degradation.

    “The RING domain possesses E3 ligase activity, stimulating poly-K63 and poly-K48 ubiquitination of the cytoplasmic tail of LDLR, thereby marking it for lysosomal degradation [65,68].”

    From The low-density lipoprotein receptor: Emerging post-transcriptional regulatory mechanisms (2025) · cites this paper as [68]

    The Abstract reports that IDOL transfers ubiquitin chains to LDLR and that either K48 or K63 linkages can target LDLR to the lysosome. The Results identify IDOL’s RING domain as catalytic. The Discussion describes ubiquitination of residues in LDLR’s cytoplasmic tail as a possibility, rather than establishing that the measured K48- and K63-linked chains are attached there. (LLM, conf=0.83)

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Metadata

Authors
Zhang, L., Xu, M., Scotti, E., Chen, Z. J., & Tontonoz, P.
Venue
Journal of Lipid Research
Publisher
Elsevier BV
Published
2013-05
Volume
54
Issue
5
Pages
1410-1420
ISSN
0022-2275
DOI
10.1194/jlr.m035774
PMC
PMC3653405
Cited by
60
References
3
Language
en
Licence

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