Opposing actions of JIP4 and RILPL1 provide antagonistic motor force to dynamically regulate membrane reformation during lysosomal tubulation/sorting driven by LRRK2 Article Swipe
Luis Bonet‐Ponce
,
Tsion Tegicho
,
Alexandra Beilina
,
Jillian H. Kluss
,
Yan Li
,
Mark Cookson
·
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1101/2024.04.02.587808
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1101/2024.04.02.587808
Lysosomes are dynamic cellular structures that adaptively remodel their membrane in response to stimuli, including membrane damage. We previously uncovered a process we term LYTL (LYsosomal Tubulation/sorting driven by Leucine-Rich Repeat Kinase 2 [LRRK2]), wherein damaged lysosomes generate tubules sorted into mobile vesicles. LYTL is orchestrated by the Parkinson’s disease-associated kinase LRRK2 that recruits the motor adaptor protein and RHD family member JIP4 to lysosomes via phosphorylated RAB proteins. To identify new players involved in LYTL, we performed unbiased proteomics on isolated lysosomes after LRRK2 kinase inhibition. Our results demonstrate that there is recruitment of RILPL1 to ruptured lysosomes via LRRK2 activity to promote phosphorylation of RAB proteins at the lysosomal surface. RILPL1, which is also a member of the RHD family, enhances the clustering of LRRK2-positive lysosomes in the perinuclear area and causes retraction of LYTL tubules, in contrast to JIP4 which promotes LYTL tubule extension. Mechanistically, RILPL1 binds to p150 Glued , a dynactin subunit, facilitating the transport of lysosomes and tubules to the minus end of microtubules. Further characterization of the tubulation process revealed that LYTL tubules move along tyrosinated microtubules, with tubulin tyrosination proving essential for tubule elongation. In summary, our findings emphasize the dynamic regulation of LYTL tubules by two distinct RHD proteins and pRAB effectors, serving as opposing motor adaptor proteins: JIP4, promoting tubulation via kinesin, and RILPL1, facilitating tubule retraction through dynein/dynactin. We infer that the two opposing processes generate a metastable lysosomal membrane deformation that facilitates dynamic tubulation events.
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Metadata
- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.1101/2024.04.02.587808
- https://www.biorxiv.org/content/biorxiv/early/2024/04/03/2024.04.02.587808.full.pdf
- OA Status
- green
- Cited By
- 5
- References
- 81
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4393901860
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4393901860Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1101/2024.04.02.587808Digital Object Identifier
- Title
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Opposing actions of JIP4 and RILPL1 provide antagonistic motor force to dynamically regulate membrane reformation during lysosomal tubulation/sorting driven by LRRK2Work title
- Type
-
preprintOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2024Year of publication
- Publication date
-
2024-04-03Full publication date if available
- Authors
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Luis Bonet‐Ponce, Tsion Tegicho, Alexandra Beilina, Jillian H. Kluss, Yan Li, Mark CooksonList of authors in order
- Landing page
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https://doi.org/10.1101/2024.04.02.587808Publisher landing page
- PDF URL
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https://www.biorxiv.org/content/biorxiv/early/2024/04/03/2024.04.02.587808.full.pdfDirect link to full text PDF
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YesWhether a free full text is available
- OA status
-
greenOpen access status per OpenAlex
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https://www.biorxiv.org/content/biorxiv/early/2024/04/03/2024.04.02.587808.full.pdfDirect OA link when available
- Concepts
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Cell biology, Dynein, Dynactin, Signal transducing adaptor protein, Microtubule, Motor protein, Biology, Kinesin, Rab, LRRK2, GTPase, Phosphorylation, Biochemistry, Gene, MutationTop concepts (fields/topics) attached by OpenAlex
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5Total citation count in OpenAlex
- Citations by year (recent)
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2025: 4, 2024: 1Per-year citation counts (last 5 years)
- References (count)
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81Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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