Adapter Proteins for Opposing Motors Interact Simultaneously with Nuclear Pore Protein Nup358 Article Swipe
Heying Cui
,
Crystal R. Noell
,
Rachael P. Behler
,
Jacqueline B. Zahn
,
Lynn R. Terry
,
Blaine B. Russ
,
Sozanne R. Solmaz
·
YOU?
·
· 2019
· Open Access
·
· DOI: https://doi.org/10.1021/acs.biochem.9b00907
YOU?
·
· 2019
· Open Access
·
· DOI: https://doi.org/10.1021/acs.biochem.9b00907
Nup358 is a protein subunit of the nuclear pore complex that recruits the opposing microtubule motors kinesin-1 and dynein [via the dynein adaptor Bicaudal D2 (BicD2)] to the nuclear envelope. This pathway is important for positioning of the nucleus during the early steps of mitotic spindle assembly and also essential for an important process in brain development. It is unknown whether dynein and kinesin-1 interact with Nup358 simultaneously or whether they compete. Here, we have reconstituted and characterized a minimal complex of kinesin-1 light chain 2 (KLC2) and Nup358. The proteins interact through a W-acidic motif in Nup358, which is highly conserved among vertebrates but absent in insects. While Nup358 and KLC2 form predominantly monomers, their interaction results in the formation of 2:2 complexes, and the W-acidic motif is required for the oligomerization. In active motor complexes, BicD2 and KLC2 each form dimers. Notably, we show that the dynein adaptor BicD2 and KLC2 interact simultaneously with Nup358, resulting in the formation of 2:2:2 complexes. Mutation of the W-acidic motif results in the formation of 1:1:1 complexes. On the basis of our data, we propose that Nup358 recruits simultaneously one kinesin-1 motor and one dynein motor via BicD2 to the nucleus. We hypothesize that the binding sites are close enough to promote direct interactions between these motor recognition domains, which may be important for the regulation of the motility of these opposing motors. Our data provide important insights into a nuclear positioning pathway that is crucial for brain development and faithful chromosome segregation.
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Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1021/acs.biochem.9b00907
- OA Status
- green
- Cited By
- 17
- References
- 69
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W2989873025
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W2989873025Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1021/acs.biochem.9b00907Digital Object Identifier
- Title
-
Adapter Proteins for Opposing Motors Interact Simultaneously with Nuclear Pore Protein Nup358Work title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
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2019Year of publication
- Publication date
-
2019-11-22Full publication date if available
- Authors
-
Heying Cui, Crystal R. Noell, Rachael P. Behler, Jacqueline B. Zahn, Lynn R. Terry, Blaine B. Russ, Sozanne R. SolmazList of authors in order
- Landing page
-
https://doi.org/10.1021/acs.biochem.9b00907Publisher landing page
- Open access
-
YesWhether a free full text is available
- OA status
-
greenOpen access status per OpenAlex
- OA URL
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https://www.ncbi.nlm.nih.gov/pmc/articles/7243271Direct OA link when available
- Concepts
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Dynein, Motor protein, Signal transducing adaptor protein, Cell biology, Nuclear pore, Microtubule, Kinesin, Biology, Biophysics, Chemistry, Nucleus, Signal transductionTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
17Total citation count in OpenAlex
- Citations by year (recent)
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2025: 3, 2024: 2, 2023: 3, 2022: 3, 2021: 3Per-year citation counts (last 5 years)
- References (count)
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69Number of works referenced by this work
- Related works (count)
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10Other works algorithmically related by OpenAlex
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