Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins.
By L. Hicke, R. Dunn. Annual Review of Cell and Developmental Biology, 2003
1,182 citations recorded by the source corpus.
View Paper: https://www.semanticscholar.org/paper/474c905e2a11af7792eaab969292ec127302e880
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Citations in the corpus
- A Proteome-wide, Quantitative Survey of In Vivo Ubiquitylation Sites Reveals Widespread Regulatory Roles (2011, background): “Ubiquitylation plays an important role in the regulation of cell surface receptor endocytosis (50).”
- Ubiquitylation and cell signaling (2005, background): “Monoubiquitylation might have several regulatory roles for the targeted protein, such as changes in subcellular localization, conformation, activity and protein interactions (Haglund et al, 2003a; Hicke and Dunn, 2003).”
- Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes (2006, unknown): “…biological roles, the Nox proteins have been implicated in several cell-fate pathways, such as the Ras mitogenic pathway (Irani et al., 1997), the MAP kinases (Gu et al., 2002; Xu et al., 2002), the JAK–STAT pathways (Schieffer et al., 2000), and NF-κB (Sulciner et al., 1996; Gu et al., 2003).”
- The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins (2009, background): “The ubiquitylation of some membrane proteins may actually serve as internalization signa”
- TRIM/RBCC, a novel class of ‘single protein RING finger’ E3 ubiquitin ligases (2005, background): “Different ubiquitin chain lengths are associated with different outcomes: while polyubiquitin chains are usually associated with proteasomal degradation, mono- and di-ubiquitination have been implicated in endocytotic processes.((4,5)) The lysine of the ubiquitin moiety used for isopeptide bond form”
- Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. (2006, background): “nalization of cell surface proteins into the endocytic pathway (17) and also can be used in the regulation of transcription (18).”
- Involvement of linear polyubiquitylation of NEMO in NF-κB activation (2009, background): “Although monoubiquitylation of proteins is common in the endocytic pathwa”
- Function and regulation in MAPK signaling pathways: lessons learned from the yeast Saccharomyces cerevisiae. (2007, background): “Since Sst2 associates tightly with pheromone receptors [354] and the receptors undergo robust constitutive and ligandinduced endocytosis in a ubiquitin-dependent manner [358], the latter interaction with proteins involved in endosomal trafficking may be physiologically significant.”
- A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules. (2006, unknown): “1000 Cell 126, 995–1004, September 8, 2006 a2006 Elsevier I to recruit the cellular proteins necessary for internalization of membrane-bound proteins (Hicke and Dunn, 2003), presumably leading to degradation of the CD8a-FKBP fusion.”
- Palmitoylation: policing protein stability and traffic (2007, background): “Ubiquitylation is also a signal that directs proteins into an endosomal compartment from either the Golgi or the plasma membrane, and the ubiquitylated proteins are subsequently sorted into multivesicular bodies that ultimately fuse with the lysosome, where these proteins are degraded by lysosomal”
- Physiological functions of the HECT family of ubiquitin ligases (2009, background): “Targets that contain Lys48-linked ubiquitin chains are usually degraded by the 26S proteasome, whereas monoubiquitylation and polyubiquitylation through Lys63 seems to be involved in a number of different cellular processes, such as endocytosis and vesicular sortin”
- Ubiquitin: structures, functions, mechanisms. (2004, background): “[17,19]), but functional understanding of these domains is still at an early stage.”
- Ubiquitin and ubiquitin-like proteins as multifunctional signals (2005, background): “The ubiquitylation of membrane proteins regulates endocytosis, multivesicular-body formation, and Golgi and endoplasmic reticulum function”