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Distinct monoubiquitin signals in receptor endocytosis
Abstract
Numerous cellular proteins are post-translationally modified by the addition of the small modifier protein ubiquitin (Ub). The functional consequences of the type of ubiquitination vary, such that polyubiquitinated proteins are targeted for degradation by the proteasome, whereas monoubiquitination is implicated in other cellular functions, including endocytic trafficking and DNA repair. The monoubiquitination of trafficking cargoes, such as receptors and associated proteins, as well as of endocytic accessory Ub-binding proteins, raises the question of the precise function of monoubiquitin signals in the endocytic route. Recent biochemical and genetic evidence shows that multiple monoubiquitination of epidermal growth factor and platelet-derived growth factor receptors provides trafficking and sorting tags that ensure receptor endocytosis and degradation, whereas monoubiquitination of accessory proteins might play a role in regulating their function as Ub-receptors in the endosome.
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Upon ligand stimulation, RTKs undergo ubiquitin-mediated internalization leading to degradation via the endosomal-lysosomal pathway.
“It is well documented that upon ligand stimulation RTKs undergo ubiquitin-mediated internalization leading to degradation via the endosomal-lysosomal pathway (13,39).”
From Essential Role of Ubiquitin-Specific Protease 8 for Receptor Tyrosine Kinase Stability and Endocytic Trafficking In Vivo (2007) · cites this paper as [13]
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Metadata
- Authors
- Haglund, K.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2003-11
- Volume
- 28
- Issue
- 11
- Pages
- 598-604
- ISSN
- 0968-0004
- Cited by
- 367
- References
- 0
- Language
- en
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