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The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
The endosomal sorting complex required for transport (ESCRT) machinery sorts cargo labelled with ubiquitin into invaginations of endosome membranes and mediates the breaking off of the cargo-containing intraluminal vesicles from the perimeter membrane.
Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes
- C. Raiborg, K. Bache, D. Gillooly, I. Madshus, E. Stang, H. Stenmark
- Biology, Computer ScienceNature Cell Biology
- 1 May 2002
It is concluded that the hepatocyte growth factor-regulated tyrosine kinase substrate, Hrs, sorts ubiquitinated membrane proteins into clathrin-coated microdomains of early endosomes, thereby preventing their recycling to the cell surface.
Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease
It is shown that autophagic degradation is inhibited in cells depleted of ESCRT subunits and in cells expressing CHMP2B mutants, leading to accumulation of protein aggregates containing ubiquitinated proteins, p62 and Alfy, and functional MVBs are required for clearance of TDP-43 and expanded polyglutamine aggregates associated with Huntington's disease.
Hrs recruits clathrin to early endosomes
- C. Raiborg, Kristi Grønvold Bache, A. Mehlum, E. Stang, H. Stenmark
- Biology, Computer ScienceThe EMBO journal
- 3 September 2001
It is shown that Hrs and EEA1, a FYVE domain protein involved in endocytic membrane fusion, are localized to different regions of early endosomes and that the C‐terminus of Hrs contains a functional clathrin box motif that interacts directly with the terminal β‐propeller domain ofClathrin heavy chain.
The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4.
FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes.
The protein was found to colocalise extensively with EEA1, an established marker of early endosomes, and the endosomal targeting of Hrs is mediated by a PtdIns(3)P-binding FYVE domain in cooperation with an additional domain.
STAM and Hrs Are Subunits of a Multivalent Ubiquitin-binding Complex on Early Endosomes*
- K. Bache, C. Raiborg, A. Mehlum, H. Stenmark
- Biology, Computer ScienceThe Journal of Biological Chemistry
- 4 April 2003
It is proposed that Hrs, Eps15, and STAM proteins function in a multivalent complex that sorts ubiquitinated proteins into the multivesicular body pathway.
Protein sorting into multivesicular endosomes.
Repeated ER–endosome contacts promote endosome translocation and neurite outgrowth
Re protrudin-containing ER–LE contact sites are platforms for kinesin-1 loading onto LEs, and kines in-1-mediated translocation of LEs to the plasma membrane, fuelled by repeated ER contacts, promotes protrusion and neurite outgrowth.