|PROSITE documentation PDOC51312|
The endosomal sorting complex required for transport (ESCRT) complexes form the machinery driving protein sorting from endosomes to lysosomes. ESCRT complexes are central to receptor downregulation, lysosome biogenesis, and budding of HIV. Yeast ESCRT-I consists of three protein subunits, VPS23, VPS28, and VPS37. In humans, ESCRT-I comprises TSG101, VPS28, and one of four potential human VPS37 homologs. The main role of ESCRT-I is to recognize ubiquitinated cargo via the UEV domain of the VPS23/TSG101 subunit. The assembly of the ESCRT-I complex is directed by the C-terminal steadiness box (SB) of VPS23, the N-terminal half of VPS28, and the C-terminal half of VPS37. The structure is primarily composed of three long, parallel helical hairpins, each corresponding to a different subunit (see <PDB:2CAZ>). The additional domains and motifs extending beyond the core serve as gripping tools for ESCRT-I critical functions [1,2].
The profiles we developed cover the entire steadiness box, VPS28 N-terminal and VPS37 C-terminal domains.Last update:
May 2007 / First entry.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Teo H. Gill D.J. Sun J. Perisic O. Veprintsev D.B. Vallis Y. Emr S.D. Williams R.L.|
|Title||ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes.|
|2||Authors||Kostelansky M.S. Sun J. Lee S. Kim J. Ghirlando R. Hierro A. Emr S.D. Hurley J.H.|
|Title||Structural and functional organization of the ESCRT-I trafficking complex.|