Rilp Interacts with Vps22 and Vps36 of Escrt-ii and Regulates Their Membrane Recruitment.
From: Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Proteos, 61 Biopolis Drive, Singapore 138673, Singapore.
Biochemical and biophysical research communications
- Publish Date: Nov 2006
- ISSN: 0006-291X
- Volume: 350
- Issue: 2
- Pages: 413-23
- Medium: Print
- Language: English
- Citation (JAMA): Wang Tuanlao, Hong Wanjin, et al. Rilp Interacts with Vps22 and Vps36 of Escrt-ii and Regulates Their Membrane Recruitment.. Biochem. Biophys. Res. Commun. Nov 2006;350:413-23
Abstract
RILP is emerging as a key regulator of late endocytic pathway by functioning as a downstream effector of activated Rab7 and Rab34, while ESCRT-I — >ESCRT-II — >ESCRT-III machinery acts in sorting proteins to the multivesicular body (MVB) initiated at the early/sorting endosome. We show here that the early machinery is integrated with the late machinery through a novel regulatory loop in which RILP interacts with VPS22 and VPS36 of ESCRT-II to mediate their membrane recruitment. The N-terminal and C-terminal half of RILP mediate interaction with VPS22 and VPS36, respectively. Overexpression of RILP leads to enlarged and clustered MVBs marked by lysobisphosphatidic acid (LBPA). In addition, RILP or its C-terminal fragment causes a retardation of sorting internalized EGF to the degradation route at the level of sorting endosomes marked by EEA1. We propose that RILP — >ESCRT-II serves as a regulatory/feedback loop to govern the coordination of early and late parts of the endocytic pathway.
Mesh Headings (Keywords): Adaptor Proteins, Signal Transducing, Binding Sites, Cytoplasm, Endocytosis, Endosomes, Epidermal Growth Factor, Hela Cells, Humans, Intracellular Membranes
Check for Full Text / PubMed Unique Identifier (PMID): 17010938
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