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PreprintCited by 22RNA Research and SplicingAmyotrophic Lateral Sclerosis ResearchRNA and protein synthesis mechanisms

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Muscleblind-like proteins use modular domains to localize RNAs by riding kinesins and docking to membranes

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Hildebrandt, Ryan P., Moss, Kathryn R., Janusz-Kaminska, Aleksandra, Knudson, Luke A., Denes, Lance T., Saxena, Tanvi, Boggupalli, Devi Prasad, Li, Zhuangyue, Lin, Kun, Bassell, Gary J., Wang, Eric T.·2022·Nature Communications
DOI 10.1101/2022.07.06.498900PMC PMC10256740

Preprint — published as 10.1038/s41467-023-38923-6

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Abstract

Summary: RNA transport and local translation provide spatial control of gene expression, and RNA binding proteins (RBPs) act as critical adapters in this multi-step process. Muscleblind-like (MBNL) RNA binding proteins, implicated in myotonic dystrophy and cancer, localize RNAs to myoblast membranes and distal neurites through unknown mechanisms. We found that MBNL forms motile and anchored granules in neurons and myoblasts, and selectively associates with kinesins Kif1bα and Kif1c through its zinc finger (ZnF) domains. Other RBPs with similar ZnFs also associate with these kinesins, implicating a motor-RBP specificity code. Live cell imaging and fractionation revealed that membrane anchoring is mediated through the unstructured carboxy-terminal tail of MBNL1. Both kinesin- and membrane-recruitment functions were reconstituted using MBNL-MS2 coat protein fusions. This approach, termed RBP Module Recruitment and Imaging (RBP-MRI), decouples RNA binding, kinesin recruitment, and membrane anchoring functions, while also establishing general strategies for studying multi-functional, modular domains of RBPs.

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Metadata

Authors
Hildebrandt, R. P., Moss, K. R., Janusz-Kaminska, A., Knudson, L. A., Denes, L. T., Saxena, T., Boggupalli, D. P., Li, Z., Lin, K., Bassell, G. J., & Wang, E. T.
Affiliations
  • University of Florida (US)
  • Emory University (US)
Corresponding author
  • Bassell, Gary J.
  • Wang, Eric T.
ORCID
Venue
Nature Communications
Publisher
openRxiv
Published
2022-07-06
Volume
14
Issue
1
Pages
3427-3427
ISSN
2041-1723 (ISSN-L)
DOI
10.1101/2022.07.06.498900
PMC
PMC10256740
OpenAlex
W4379980526
Cited by
22
References
1
Citations by year
2026: 6 · 2025: 9 · 2024: 6 · 2023: 1
FWCI
1.95
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • U.S. Department of Health and Human Services (R01 NS114253)
  • Massachusetts Institute of Technology
  • Emory University
  • Chan Zuckerberg Initiative
  • National Institutes of Health (NIH-R01)
  • University at Albany
  • National Institute of Neurological Disorders and Stroke (F31NS117086, R01NS114253)
  • Institute of Genetics
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
muscleblind-like proteins, RNA-binding proteins, RNA localization, kinesin, KIF1C, zinc finger, membrane anchoring, C-terminal tail, nucleolin, myoblasts, neurites, myotonic dystrophy, modular protein domains
MeSH terms
Humans, Myotonic Dystrophy, RNA, RNA, Messenger, Kinesins, Alternative Splicing

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