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RILP encodes a lysosomal protein that interacts with RAB7, a small GTPase that controls transport to endocytic degradative compartments. Zusätzlich bieten wir Ihnen RILP Antikörper (18) und RILP Kits (2) und viele weitere Produktgruppen zu diesem Protein an.
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RILP suppresses the invasion of breast cancer cells by interacting with RalGDS (zeige RALGDS Proteine) to inhibit its guanine nucleotide exchange factor (zeige RASGRF1 Proteine) activity for RalA (zeige rala Proteine).
RILP regulates vacuolar ATPase through interaction with the V1G1 subunit
VPS41 (zeige VPS41 Proteine) subunit of HOPS (zeige ALPL Proteine) complex was defined to be the major partner for interacting with RILP.
RILP regulates the activity of the V-ATPase (zeige ATP6V1H Proteine) through its interaction with V1G1.
RILP directly and concomitantly binds the tethering HOPS (zeige ALPL Proteine) complex and the p150(Glued (zeige DCTN1 Proteine)) subunit of the dynein motor. ORP1L then functions as a cholesterol-sensing switch controlling RILP-HOPS (zeige ALPL Proteine)-p150(Glued (zeige DCTN1 Proteine)) interactions.
Unique region in RILP responsible for its specific role in regulating lysosomal morphology as well as in its interaction with Rab7 (zeige RAB7B Proteine) and Rab34 (zeige RAB34 Proteine).
The crystal structure of Rab7 (zeige RAB7B Proteine)-GTP (zeige AK3 Proteine) in complex with the Rab7 (zeige RAB7B Proteine) binding domain of RILP reveals that Rab7 (zeige RAB7B Proteine) interacts with RILP specifically via two distinct areas.
The data together indicate that RILP, as already demonstrated for several other Rab (zeige HRB Proteine) 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.
Hence, RILPsv provides an extra dimension to the control of vesicle fusion and transport by the small GTPase (zeige RACGAP1 Proteine) Rab7 (zeige RAB7B Proteine).
The up-regulation of Rab11 (zeige RAB11A Proteine), Rab7 (zeige RAB7A Proteine), or RILP, but not its truncated form RILP-C33 (zeige CD82 Proteine), rescued LAMP2A-defective trafficking in cystinosis, whereas dominant-negative Rab11 (zeige RAB11A Proteine) or Rab7 (zeige RAB7A Proteine) impaired LAMP2A trafficking.
A new mechanism by which the dynein-dynactin (zeige DCTN1 Proteine) motor complex recognizes Mreg (zeige MREG Proteine) on mature melanosomes is revealed through interaction with RILP and is involved in the centripetal movement of melanosomes.
Rab36 (zeige RAB36 Proteine) mediates retrograde melanosome transport in melanocytes through interaction with RILP.
CD63 (zeige CD63 Proteine), but not RILP, is recruited to the phagosomes in macrophages expressing the dominant negative form of Rab7 (zeige RAB7A Proteine).
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