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RILP encodes a lysosomal protein that interacts with RAB7, a small GTPase that controls transport to endocytic degradative compartments. Additionally we are shipping RILP Antibodies (19) and RILP Proteins (3) and many more products for this protein.
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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.
RILP suppresses the invasion of breast cancer cells by interacting with RalGDS (show RALGDS ELISA Kits) to inhibit its guanine nucleotide exchange factor (show RASGRF1 ELISA Kits) activity for RalA (show rala ELISA Kits).
RILP regulates vacuolar ATPase (show DNAH8 ELISA Kits) through interaction with the V1G1 subunit
VPS41 subunit of HOPS (show ALPL ELISA Kits) complex was defined to be the major partner for interacting with RILP.
RILP regulates the activity of the V-ATPase through its interaction with V1G1.
RILP directly and concomitantly binds the tethering HOPS (show ALPL ELISA Kits) complex and the p150(Glued (show DCTN1 ELISA Kits)) subunit of the dynein motor. ORP1L then functions as a cholesterol-sensing switch controlling RILP-HOPS (show ALPL ELISA Kits)-p150(Glued (show DCTN1 ELISA Kits)) interactions.
Unique region in RILP responsible for its specific role in regulating lysosomal morphology as well as in its interaction with Rab7 and Rab34.
The crystal structure of Rab7-GTP (show AK3 ELISA Kits) in complex with the Rab7 binding domain of RILP reveals that Rab7 interacts with RILP specifically via two distinct areas.
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.
RILP indeed prenylated, while phosphorylation analysis showed that the two protein kinase A sites are phosphorylated.
The up-regulation of Rab11 (show RAB11A ELISA Kits), Rab7 (show RAB7A ELISA Kits), or RILP, but not its truncated form RILP-C33 (show CD82 ELISA Kits), rescued LAMP2A-defective trafficking in cystinosis, whereas dominant-negative Rab11 (show RAB11A ELISA Kits) or Rab7 (show RAB7A ELISA Kits) impaired LAMP2A trafficking.
A new mechanism by which the dynein-dynactin (show DCTN1 ELISA Kits) motor complex recognizes Mreg on mature melanosomes is revealed through interaction with RILP and is involved in the centripetal movement of melanosomes.
Rab36 mediates retrograde melanosome transport in melanocytes through interaction with RILP.
CD63 (show CD63 ELISA Kits), but not RILP, is recruited to the phagosomes in macrophages expressing the dominant negative form of Rab7 (show RAB7A ELISA Kits).
This gene encodes a lysosomal protein that interacts with RAB7, a small GTPase that controls transport to endocytic degradative compartments. Studies using mutant forms of the two proteins suggest that this protein represents a downstream effector for RAB7, and both proteins act together in the regulation of late endocytic traffic. A unique region of this protein has also been shown to be involved in the regulation of lysosomal morphology.
Rab interacting lysosomal protein
, rab-interacting lysosomal protein