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p116Rip is a novel filamentous actin-binding protein
Jacqueline Mulder1, Mieke Poland, Martijn F B G Gebbink
1Division of Cellular Biochemistry and Centre for Biomedical Genetics, The Netherlands Cancer Institute, Amsterdam.
The Journal of Biological Chemistry
|May 7, 2003
Summary
p116Rip is a filamentous actin (F-actin)-binding protein that disassembles the actomyosin cytoskeleton. It bundles F-actin in vitro and disrupts stress fibers in vivo, impacting cell morphology and lamellipodia formation.
Area of Science:
- Cell Biology
- Cytoskeleton Dynamics
- Protein Biochemistry
Background:
- p116Rip was identified as a RhoA binding partner.
- Its function remained largely unknown.
- Overexpression inhibits RhoA-mediated cell contraction.
Purpose of the Study:
- To elucidate the function of p116Rip.
- To determine its interaction with the cytoskeleton.
- To investigate its role in cell morphology.
Main Methods:
- Immunofluorescence microscopy to determine localization.
- Yeast two-hybrid and co-immunoprecipitation assays for protein interactions.
- In vitro F-actin binding and bundling assays.
- Expression studies in NIH3T3 cells.
Main Results:
- p116Rip localizes to F-actin structures and the nucleus.
- It binds F-actin tightly via its N-terminal region.
- p116Rip bundles F-actin in vitro and disrupts stress fibers in vivo.
- Overexpression inhibits lamellipodia formation.
Conclusions:
- p116Rip is an F-actin-binding protein with bundling activity.
- It plays a role in disassembling the actomyosin cytoskeleton.
- p116Rip influences cell shape and cytoskeletal organization.