ArticleThe Journal of biological chemistry2012
The Rab interacting lysosomal protein (RILP) homology domain functions as a novel effector domain for small GTPase Rab36: Rab36 regulates retrograde melanosome transport in melanocytes.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 97 citations in OpenAlex.
- Late Endosome Transport by RILP-RAB7A Promotes Dendrite Arborization Independently of Degradation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026Article
- Ultrastructural studies reveal a new role for JIP3/MAPK8IP3 in endo-lysosomal maturation within the neuronal cell body.Molecular biology of the cell · 2026Article
- A Syd and RUFY dynein adaptor complex mediates axonal circulation of dense core vesicles.The Journal of cell biology · 2026Article
- The Functions of RAB GTPases at the Golgi Complex.Sub-cellular biochemistry · 2026Review
- Late endosome transport by RILP-RAB7A promotes dendrite arborization.bioRxiv : the preprint server for biology · 2025Article
- Melanosome Transport and Processing in Skin Pigmentation: Mechanisms and Targets for Pigmentation Modulation.International journal of molecular sciences · 2025Review
- Phosphorylation-driven effector switching of Rab7 and Rab12 by the leucine-rich repeat kinase 1 in mast cells.Frontiers in immunology · 2025Article
- Engine breakdown of lysosomes and related organelles and the resulting physiology.Frontiers in cell and developmental biology · 2025Review
- Biogenesis and homeostasis of mast cell lysosome related secretory granules.Frontiers in cell and developmental biology · 2025Review
- Disruptions in axonal lysosome transport and its contribution to neurological disease.Current opinion in cell biology · 2024Review
- Localization, traffic and function of Rab34 in adipocyte lipid and endocrine functions.Journal of biomedical science · 2024Article
- The biochemistry of melanogenesis: an insight into the function and mechanism of melanogenesis-related proteins.Frontiers in molecular biosciences · 2024Review
- RILP inhibits tumor progression in osteosarcoma via Grb10-mediated inhibition of the PI3K/AKT/mTOR pathway.Molecular medicine (Cambridge, Mass.) · 2023Article
- Melanin's Journey from Melanocytes to Keratinocytes: Uncovering the Molecular Mechanisms of Melanin Transfer and Processing.International journal of molecular sciences · 2023Review
- A Comprehensive Review of Mammalian Pigmentation: Paving the Way for Innovative Hair Colour-Changing Cosmetics.Biology · 2023Review
- Axonal transport of autophagosomes is regulated by dynein activators JIP3/JIP4 and ARF/RAB GTPases.bioRxiv : the preprint server for biology · 2023Article
- RILPL2 is associated with the progression and prognosis of cervical squamous cell carcinoma and endocervical adenocarcinoma.American journal of translational research · 2023Article
- TBC1D18 is a Rab5-GAP that coordinates endosome maturation together with Mon1.The Journal of cell biology · 2022Article
- LRRK2 recruitment, activity, and function in organelles.The FEBS journal · 2022Review
- The type V myosin-containing complex HUM is a RAB11 effector powering movement of secretory vesicles.iScience · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small GTPase Rab functions as a molecular switch that drives membrane trafficking through specific interaction with its effector molecule. Thus, identification of its specific effector domain is crucial to revealing the molecular mechanism that underlies Rab-mediated membrane trafficking. Because of the large numbers of Rab isoforms in higher eukaryotes, however, the effector domains of most of the vertebrate- or mammalian-specific Rabs have yet to be determined. In this study we screened for effector molecules of Rab36, a previously uncharacterized Rab isoform that is largely conserved in vertebrates, and we succeeded in identifying nine Rab36-binding proteins, including RILP (Rab interacting lysosomal protein) family members. Sequence comparison revealed that five of nine Rab36-binding proteins, i.e. RILP, RILP-L1, RILP-L2, and JIP3/4, contain a conserved coiled-coil domain. We identified the coiled-coil domain as a RILP homology domain (RHD) and characterized it as a common Rab36-binding site. Site-directed mutagenesis of the RHD of RILP revealed the different contributions by amino acids in the RHD to binding activity toward Rab7 and Rab36. Expression of RILP in melanocytes, but not expression of its Rab36 binding-deficient mutants, induced perinuclear aggregation of melanosomes, and this effect was clearly attenuated by knockdown of endogenous Rab36 protein. Moreover, knockdown of Rab36 in Rab27A-deficient melanocytes, which normally exhibit perinuclear melanosome aggregation because of increased retrograde melanosome transport activity, caused dispersion of melanosomes from the perinucleus to the cell periphery, but knockdown of Rab7 did not. Our findings indicated that Rab36 mediates retrograde melanosome transport in melanocytes through interaction with RILP.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.