Demultiplexing overlapping signaling scaffold functions to probe lipid messenger coupling to cytoskeletal dynamics Article Swipe
Nicholaus J. Trenton
,
Robert T. McLaughlin
,
Satya Bellamkonda
,
David Tsao
,
Emily M. Mace
,
Jordan S. Orange
,
Volker Schweikhard
,
Michael Diehl
·
YOU?
·
· 2019
· Open Access
·
· DOI: https://doi.org/10.1101/657049
YOU?
·
· 2019
· Open Access
·
· DOI: https://doi.org/10.1101/657049
The coordination of lipid messenger signaling with cytoskeletal regulation is central to many organelle-specific signaling and regulatory processes. While central to many aspects of cell physiology, this coupling often depends on the function of multi-domain scaffolds that orchestrate transient interactions and dynamic feedback among a spectrum of signaling intermediates and regulatory proteins on organelles. Understanding scaffold protein functions has remained challenging given this complexity. This work employs live-cell imaging and statistical analyses to deconvolve (demultiplex) how the multi-domain scaffold IQGAP1 coordinates phosphoinositide signaling with organelle-specific actin regulation and membrane processing events. Using actin-ensconced endosomes that localize to the basal cortex of polarized epithelial cells as a model system, we demonstrate abilities to dissect how IQGAP1 transitions between different actin and endosomal-membrane tethered states. We provide evidence IQGAP1 functions as a transient inhibitor of actin growth around the endosomes in at least one of these states. While not easily distilled via standard (static) colocalization analyses or traditional pathway perturbations methods, this negative regulation was revealed via a series of dynamic correlation and multiple regression analyses. These methods also uncovered that the negative actin regulation is linked to GTPase-dependent tethering to the endosomal membrane. Moreover, the scaffold transitions underlying this control are shown to depend on the production of PIP 3 lipid messengers by the lipid kinase PI3K. Overall, these methods and results provide new insights in to how IQGAP1 act as a signaling hub by orchestrating time-dependent membrane and cytoskeletal protein interactions and provide new routes to dissect scaffold-mediated pathway regulation in a variety of settings.
Related Topics
Concepts
Cell biology
Scaffold protein
Cytoskeleton
Endosome
Second messenger system
Biology
Actin cytoskeleton
Actin
Organelle
Actin remodeling
Colocalization
Signal transduction
Cell
Biochemistry
Intracellular
Metadata
- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.1101/657049
- https://www.biorxiv.org/content/biorxiv/early/2019/06/14/657049.full.pdf
- OA Status
- green
- References
- 35
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W2950568972
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W2950568972Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1101/657049Digital Object Identifier
- Title
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Demultiplexing overlapping signaling scaffold functions to probe lipid messenger coupling to cytoskeletal dynamicsWork title
- Type
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preprintOpenAlex work type
- Language
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enPrimary language
- Publication year
-
2019Year of publication
- Publication date
-
2019-06-14Full publication date if available
- Authors
-
Nicholaus J. Trenton, Robert T. McLaughlin, Satya Bellamkonda, David Tsao, Emily M. Mace, Jordan S. Orange, Volker Schweikhard, Michael DiehlList of authors in order
- Landing page
-
https://doi.org/10.1101/657049Publisher landing page
- PDF URL
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https://www.biorxiv.org/content/biorxiv/early/2019/06/14/657049.full.pdfDirect link to full text PDF
- Open access
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YesWhether a free full text is available
- OA status
-
greenOpen access status per OpenAlex
- OA URL
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https://www.biorxiv.org/content/biorxiv/early/2019/06/14/657049.full.pdfDirect OA link when available
- Concepts
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Cell biology, Scaffold protein, Cytoskeleton, Endosome, Second messenger system, Biology, Actin cytoskeleton, Actin, Organelle, Actin remodeling, Colocalization, Signal transduction, Cell, Biochemistry, IntracellularTop concepts (fields/topics) attached by OpenAlex
- Cited by
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0Total citation count in OpenAlex
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35Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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