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Activation of endosomal dynein motors by stepwise assembly of Rab7–RILP–p150Glued, ORP1L, and the receptor βlll spectrin
Open accessAbstract
The small GTPase Rab7 controls late endocytic transport by the minus end–directed motor protein complex dynein–dynactin, but how it does this is unclear. Rab7-interacting lysosomal protein (RILP) and oxysterol-binding protein–related protein 1L (ORP1L) are two effectors of Rab7. We show that GTP-bound Rab7 simultaneously binds RILP and ORP1L to form a RILP–Rab7–ORP1L complex. RILP interacts directly with the C-terminal 25-kD region of the dynactin projecting arm p150Glued, which is required for dynein motor recruitment to late endocytic compartments (LEs). Still, p150Glued recruitment by Rab7–RILP does not suffice to induce dynein-driven minus-end transport of LEs. ORP1L, as well as βIII spectrin, which is the general receptor for dynactin on vesicles, are essential for dynein motor activity. Our results illustrate that the assembly of microtubule motors on endosomes involves a cascade of linked events. First, Rab7 recruits two effectors, RILP and ORP1L, to form a tripartite complex. Next, RILP directly binds to the p150Glued dynactin subunit to recruit the dynein motor. Finally, the specific dynein motor receptor Rab7–RILP is transferred by ORP1L to βIII spectrin. Dynein will initiate translocation of late endosomes to microtubule minus ends only after interacting with βIII spectrin, which requires the activities of Rab7–RILP and ORP1L.
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“Retrograde movement is regulated by Rab7 and its effector RILP. RILP interacts with the p150-glued subunit of dynactin, thus recruiting the minus-end-directed microtubule motor dynein to lysosomes23–25.”
From TFEB regulates lysosomal positioning by modulating TMEM55B expression and JIP4 recruitment to lysosomes (2017) · cites this paper as [24]
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“Downstream effector proteins of Rab7A include the Rab-interacting lysosomal protein (RILP), which links the phagosomal membrane to a motor complex consisting of dynein and dynactin through stepwise recruitment of p150Glued, ORP1L, and the receptor βlll spectrin (33, 34).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [33]
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Metadata
- Authors
- Johansson, M., Rocha, N., Zwart, W., Jordens, I., Janssen, L., Kuijl, C., Olkkonen, V. M., & Neefjes, J.
- Affiliations
- 1Department of Molecular Medicine, National Public Health Institute, Biomedicum, FI-00251 Helsinki, Finland
- The Netherlands Cancer Institute (NL)
- Corresponding author
- Neefjes, Jacques
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2007-02-05
- Volume
- 176
- Issue
- 4
- Pages
- 459-471
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2063981
- OpenAlex
- W2153698618
- Cited by
- 505
- References
- 48
- Citations by year
- 2026: 6 · 2025: 21 · 2024: 19 · 2023: 21 · 2022: 32 · 2021: 26 · 2020: 30 · 2019: 29 · 2018: 36 · 2017: 34 · 2016: 32 · 2015: 24 · 2014: 32 · 2013: 23 · 2012: 35
- FWCI
- 10.76
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- Rab7, RILP, p150Glued, dynactin, dynein motor, late endosomes, endosomal transport, microtubule motor proteins, GTPase effectors
- MeSH terms
- Dynactin Complex, rab7 GTP-Binding Proteins, Oxysterol Binding Proteins, Carrier Proteins, Dyneins, Endocytosis, HeLa Cells, Humans, Microtubule-Associated Proteins, Microtubules, Models, Molecular, Receptors, Steroid, Endosomes, Spectrin, Signal Transduction, Molecular Motor Proteins, rab GTP-Binding Proteins, Protein Transport, Macromolecular Substances, Adaptor Proteins, Signal Transducing
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