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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 (18) and RILP Kits (2) 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 (show RAB7B Proteins))-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 Proteins) to inhibit its guanine nucleotide exchange factor (show RASGRF1 Proteins) activity for RalA (show rala Proteins).
RILP regulates vacuolar ATPase through interaction with the V1G1 subunit
VPS41 (show VPS41 Proteins) subunit of HOPS (show ALPL Proteins) complex was defined to be the major partner for interacting with RILP.
RILP regulates the activity of the V-ATPase (show ATP6V1H Proteins) through its interaction with V1G1.
RILP directly and concomitantly binds the tethering HOPS (show ALPL Proteins) complex and the p150(Glued (show DCTN1 Proteins)) subunit of the dynein motor. ORP1L then functions as a cholesterol-sensing switch controlling RILP-HOPS (show ALPL Proteins)-p150(Glued (show DCTN1 Proteins)) interactions.
Unique region in RILP responsible for its specific role in regulating lysosomal morphology as well as in its interaction with Rab7 (show RAB7B Proteins) and Rab34 (show RAB34 Proteins).
The crystal structure of Rab7 (show RAB7B Proteins)-GTP (show AK3 Proteins) in complex with the Rab7 (show RAB7B Proteins) binding domain of RILP reveals that Rab7 (show RAB7B Proteins) interacts with RILP specifically via two distinct areas.
The data together indicate that RILP, as already demonstrated for several other Rab (show HRB Proteins) 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 Proteins), Rab7 (show RAB7A Proteins), or RILP, but not its truncated form RILP-C33 (show CD82 Proteins), rescued LAMP2A-defective trafficking in cystinosis, whereas dominant-negative Rab11 (show RAB11A Proteins) or Rab7 (show RAB7A Proteins) impaired LAMP2A trafficking.
A new mechanism by which the dynein-dynactin (show DCTN1 Proteins) motor complex recognizes Mreg (show MREG Proteins) on mature melanosomes is revealed through interaction with RILP and is involved in the centripetal movement of melanosomes.
Rab36 (show RAB36 Proteins) mediates retrograde melanosome transport in melanocytes through interaction with RILP.
CD63 (show CD63 Proteins), but not RILP, is recruited to the phagosomes in macrophages expressing the dominant negative form of Rab7 (show RAB7A Proteins).
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