In a recent paper in Traffic, Lene Malerød, a postdoc in Stenmark’s lab, shows that the ESCRT-II complex is required for degradation of ubiquitinated epidermal growth factor receptor and chemokine receptors. This provides new insight into how growth factor and chemokine receptors are transported intracellularly and identifies a novel potential tumour suppressor complex.
Binding of growth factors and cytokines to their cognate receptors on cell membranes triggers their endocytosis and degradation in lysosomes, thus providing a physiologically important negative feedback mechanism for cell signalling.
The ESCRT-II complex recognizes ubiquitinated receptors in the endosomal membrane, thus initiating their sorting to degradative lysosomes. (click to enlarge image)It is not known in detail how endocytosed receptors are trafficked to the degradative lysosomes, but work in Harald StenmarkÂ’s lab has uncovered several factors involved in this process. Among these are the so-called endosomal sorting complexes required for transport (ESCRTs), and Thomas Slagsvold in StenmarkÂ’s group has previously shown that the so-called GLUE domain in the ESCRT-II complex binds ubiquitin .
In a recent paper in Traffic, Lene Malerød, a postdoc in Stenmark’s lab, shows that the ESCRT-II complex is required for degradation of ubiquitinated epidermal growth factor receptor and chemokine receptors. This provides new insight into how growth factor and chemokine receptors are transported intracellularly and identifies a novel potential tumour suppressor complex.
From major journals, first or last author from the Institute for Cancer Research
Skotland T, Geir Iversen T, Llorente A, Sandvig K(2022) Biodistribution, pharmacokinetics and excretion studies of intravenously injected nanoparticles and extracellular vesicles: Possibilities and challenges Adv Drug Deliv Rev, 114326(in press) DOI 10.1016/j.addr.2022.114326, PubMed 35588953
Ianevski A, Giri AK, Aittokallio T(2022) SynergyFinder 3.0: an interactive analysis and consensus interpretation of multi-drug synergies across multiple samples Nucleic Acids Res(in press) DOI 10.1093/nar/gkac382, PubMed 35580060
Kidd SG, Bogaard M, Carm KT, Bakken AC, Maltau AMV, Løvf M, Lothe RA, Axcrona K, Axcrona U, Skotheim RI(2022) In situ expression of ERG protein in the context of tumor heterogeneity identifies prostate cancer patients with inferior prognosis Mol Oncol(in press) DOI 10.1002/1878-0261.13225, PubMed 35574900
Smirnov P, Smith I, Safikhani Z, Ba-Alawi W, Khodakarami F, Lin E, Yu Y, Martin S, Ortmann J, Aittokallio T, Hafner M, Haibe-Kains B(2022) Evaluation of statistical approaches for association testing in noisy drug screening data BMC Bioinformatics, 23(1), 188 DOI 10.1186/s12859-022-04693-z, PubMed 35585485
Ianevski A, Giri AK, Aittokallio T(2022) SynergyFinder 3.0: an interactive analysis and consensus interpretation of multi-drug synergies across multiple samples Nucleic Acids Res(in press) DOI 10.1093/nar/gkac382, PubMed 35580060
Skotland T, Geir Iversen T, Llorente A, Sandvig K(2022) Biodistribution, pharmacokinetics and excretion studies of intravenously injected nanoparticles and extracellular vesicles: Possibilities and challenges Adv Drug Deliv Rev, 114326(in press) DOI 10.1016/j.addr.2022.114326, PubMed 35588953
