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RILP interacts with the VPS22 component of the ESCRT-II complex
- Source :
- Biochemical and Biophysical Research Communications. 347:1074-1079
- Publication Year :
- 2006
- Publisher :
- Elsevier BV, 2006.
-
Abstract
- The Rab-interacting lysosomal protein (RILP) has been identified as an effector for the small GTPases Rab7 and Rab34. It has been demonstrated that Rab7 and RILP are key proteins for the biogenesis of lysosomes and phagolysosomes. Indeed, expression of dominant negative mutants of Rab7 or of the C-terminal half of RILP impairs biogenesis and function of these organelles. In this study we have isolated, using the yeast two-hybrid system, the EAP30/SNF8/VPS22 subunit of the ESCRT-II complex as a RILP interacting protein. We demonstrated that VPS22 interacts with the N-terminal half of RILP. The interaction data obtained with the two-hybrid system were confirmed by co-immunoprecipitation. In addition, confocal immunofluorescence revealed colocalization of GFP-RILP and HA-VPS22. These data suggest that RILP could have a role in the biogenesis of multivesicular bodies.
- Subjects :
- Multivesicular bodie
Saccharomyces cerevisiae Proteins
Protein subunit
Mutant
Biophysics
Endosomes
GTPase
Biology
Biochemistry
ESCRT II complex
Two-Hybrid System Techniques
Rab protein
Organelle
Humans
Immunoprecipitation
Molecular Biology
Adaptor Proteins, Signal Transducing
Microscopy, Confocal
Endosomal Sorting Complexes Required for Transport
Effector
Colocalization
Cell Biology
Protein Structure, Tertiary
Cell biology
endocytosi
Microscopy, Fluorescence
Multiprotein Complexes
RILP
receptor degradation
Biogenesis
HeLa Cells
VPS22
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 347
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....6d11ad96b34e97266ffa754a3ce6f01e