STIP1/HOP Regulates the Actin Cytoskeleton through Interactions with Actin and Changes in Actin-Binding Proteins Cofilin and Profilin
| Autor: | Matodzi Portia Makhubu, Adrienne L. Edkins, Abantika Chakraborty, Ianthe Wingate, Duncan Kyle Ruck, Jo-Anne de la Mare, Morgan Campbell Hunter, Sarah N. Kituyi, Gregory L. Blatch, Robert Pierre Rousseau, Samantha Joy Beckley, Kelly Schwarz |
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| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular Protein Conformation Fluorescent Antibody Technique STI1 ATPase activity lcsh:Chemistry Profilins Cytoskeleton lcsh:QH301-705.5 Heat-Shock Proteins Spectroscopy biology HOP Chemistry Microfilament Proteins STIP1 Cell migration General Medicine Cofilin Computer Science Applications Cell biology Actin Cytoskeleton Actin Depolymerizing Factors Profilin actin Protein Binding cofilin macromolecular substances Article Catalysis Inorganic Chemistry Structure-Activity Relationship Humans Protein Interaction Domains and Motifs profilin Amino Acid Sequence Actin-binding protein Physical and Theoretical Chemistry Molecular Biology Actin Organic Chemistry Actin cytoskeleton Actins lcsh:Biology (General) lcsh:QD1-999 Chaperone (protein) biology.protein Molecular Chaperones |
| Zdroj: | International Journal of Molecular Sciences Volume 21 Issue 9 International Journal of Molecular Sciences, Vol 21, Iss 3152, p 3152 (2020) |
| ISSN: | 1422-0067 |
| DOI: | 10.3390/ijms21093152 |
| Popis: | Cell migration plays a vital role in both health and disease. It is driven by reorganization of the actin cytoskeleton, which is regulated by actin-binding proteins cofilin and profilin. Stress-inducible phosphoprotein 1 (STIP1) is a well-described co-chaperone of the Hsp90 chaperone system, and our findings identify a potential regulatory role of STIP1 in actin dynamics. We show that STIP1 can be isolated in complex with actin and Hsp90 from HEK293T cells and directly interacts with actin in vitro via the C-terminal TPR2AB-DP2 domain of STIP1, potentially due to a region spanning two putative actin-binding motifs. We found that STIP1 could stimulate the in vitro ATPase activity of actin, suggesting a potential role in the modulation of F-actin formation. Interestingly, while STIP1 depletion in HEK293T cells had no major effect on total actin levels, it led to increased nuclear accumulation of actin, disorganization of F-actin structures, and an increase and decrease in cofilin and profilin levels, respectively. This study suggests that STIP1 regulates the cytoskeleton by interacting with actin, or via regulating the ratio of proteins known to affect actin dynamics. |
| Databáze: | OpenAIRE |
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