RILP interacts with the VPS22 component of the ESCRT-II complex
| Autor: | Cecilia Bucci, Azzurra De Luca, Maria Rita Spinosa, Cinzia Progida |
|---|---|
| Přispěvatelé: | Progida, C, Spinosa, MARIA RITA, DE LUCA, Azzurra, Bucci, Cecilia |
| Rok vydání: | 2006 |
| Předmět: |
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 |
| Zdroj: | Biochemical and Biophysical Research Communications. 347:1074-1079 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2006.07.007 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect