RILP Antibody, HRP conjugated

1. Hepatitis C virus (HCV) modifies cellular trafficking by cleaving Rab interacting lysosomal protein (RILP), which serves to redirect ras-related protein Rab-7 (Rab7)-containing vesicles to a kinesin-dependent trafficking mode promoting virion secretion. PMID: 27791088
2. RILP suppresses the invasion of breast cancer cells by interacting with RalGDS to inhibit its guanine nucleotide exchange factor activity for RalA. PMID: 26469971
3. RILP regulates vacuolar ATPase through interaction with the V1G1 subunit PMID: 26180254
4. VPS41 subunit of HOPS complex was defined to be the major partner for interacting with RILP. PMID: 25445562
5. RILP regulates the activity of the V-ATPase through its interaction with V1G1. PMID: 24762812
6. RILP directly and concomitantly binds the tethering HOPS complex and the p150(Glued) subunit of the dynein motor. ORP1L then functions as a cholesterol-sensing switch controlling RILP-HOPS-p150(Glued) interactions. PMID: 23729732
7. Unique region in RILP responsible for its specific role in regulating lysosomal morphology as well as in its interaction with Rab7 and Rab34. PMID: 14668488
8. The crystal structure of Rab7-GTP in complex with the Rab7 binding domain of RILP reveals that Rab7 interacts with RILP specifically via two distinct areas. PMID: 15933719
9. The data together indicate that RILP, as already demonstrated for several other Rab effector proteins, is capable of self-association, thus probably forming a homo-dimer. PMID: 15996637
10. RILP indeed prenylated, while phosphorylation analysis showed that the two protein kinase A sites are phosphorylated. PMID: 16417580
11. Hence, RILPsv provides an extra dimension to the control of vesicle fusion and transport by the small GTPase Rab7. PMID: 16631113
12. we have isolated, using the yeast two-hybrid system, the EAP30/SNF8/VPS22 subunit of the ESCRT-II complex as a RILP interacting protein. PMID: 16857164
13. These results establish that RILP is required for biogenesis of multivesicular endosomes and degradative trafficking of EGFRs but not for trafficking of transferrin receptors through early endosomes. PMID: 17959629
14. REST/NRSF, dynactin p150(Glued), huntingtin, HAP1, and RILP form a complex involved in the translocation of REST/NRSF into the nucleus and HAP1 controls REST/NRSF cellular localization in neurons PMID: 18922795
15. Results describe how ORP1L contacts VAP to control Rab7-RILP-p150 Glued and late endosome positioning. PMID: 19564404

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HGNC: 30266

OMIM: 607848

KEGG: hsa:83547

STRING: 9606.ENSP00000301336

UniGene: Hs.534497