Basic Information:
Symbol | RILP |
Synonyms | PP10141 |
Protein Name | Rab-interacting lysosomal protein |
Species | Human |
Entrez ID | 29448 |
Uniprot ID | Q96NA2 |
Membrane Contact Site |
ER-Endosome; Endosome-ER
|
Location (from literature) | Endosome |
Cell line/Tissue | MelJuSo cells |
Experimental Method | Low throughput experimental methods |
Protein Sequence | |
More related results |
Complex Information:
Complex ID | Subunit of complex | Subcellular location | Species | More |
CMCS00027 | VAPB; VAPA; OSBPL1A; RAB7A; RILP | ER-Endosome; Endosome-ER | Human | more |
Homology Information of RILP:
Uniprot ID | Q96NA2 |
EggNOG | ENOG502RXH1 |
HOGENOM | CLU_044133_1_0_1 |
OrthoDB | 5400045at2759 |
TreeFam | TF313489 |
GeneTree | ENSGT00940000161117 |
References:
Pubmed ID | 19564404 |
DOI | 10.1083/jcb.200811005 |
Description | We show that cholesterol in LEs is sensed by ORP1L, which transmits this information to the Rab7–RILP–p150Glued complex through the formation of ER–LE membrane contact sites (MCSs). At these sites, the ER protein VAP enters the Rab7–RILP complex to control p150Glued binding and positioning of LEs. |
Description of experimental evidence | The protein was validated by microscopy, FLIM, Immuno-EM and filipin stainings in MelJuSo cells, and these data explain how the ER and cholesterol control the association of LEs with motor proteins and their positioning in cells. |
More related results |