ArticleMolecular biology of the cell2007
Talin influences the dynamics of the myosin VII-membrane interaction.
Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- The filopodial myosin DdMyo7 is a slow, calcium-regulated motor.The Journal of biological chemistry · 2025Article
- Deafness mutation in the MYO3A motor domain impairs actin protrusion elongation mechanism.Molecular biology of the cell · 2022Article
- Adhesion ofFrontiers in cell and developmental biology · 2022Review
- Article
- Optimized filopodia formation requires myosin tail domain cooperation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- MyTH4-FERM myosins have an ancient and conserved role in filopod formation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Involvement of unconventional myosin VI in myoblast function and myotube formation.Histochemistry and cell biology · 2015Article
- Talin couples the actomyosin cortex to the plasma membrane during rear retraction and cytokinesis.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Characterization of a myosin VII MyTH/FERM domain.Journal of molecular biology · 2011Article
- FRAP analysis of chemosensory components of Dictyostelium.Methods in molecular biology (Clifton, N.J.) · 2009Article
- Role of nonmuscle myosin IIB and N-RAP in cell spreading and myofibril assembly in primary mouse cardiomyocytes.Cell motility and the cytoskeleton · 2008Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myosin VII (M7) and talin are ancient and ubiquitous actin-binding proteins with conserved roles in adhesion. Talin serves to link membrane receptors to the underlying actin cytoskeleton and forms a complex with M7 in Dictyostelium. The levels of talinA are tightly linked to M7 levels in Dictyostelium. Cells lacking M7 exhibit an 80% decrease in steady-state levels of talinA, whereas increased levels of M7 result in concomitant increases in total talinA. In contrast, changes in talinA levels do not affect M7 levels. Immunoprecipitation reveals that talinA and M7 are associated with each other in membrane fractions. Fluorescence recovery after photobleaching experiments on green fluorescent protein (GFP)-M7 cells expressing different levels of the M7 and talinA show that changes in the overall amounts of these two proteins influences the dynamics of membrane-associated M7. The recovery of GFP-M7 on the membrane is faster in cells lacking talinA and limited in the presence of excess amounts of talinA and M7. These results establish that M7 stabilizes talinA in the cytosol and, in return, talinA regulates the residence time of M7 at the plasma membrane, suggesting that these two proteins are both part of the same dynamic adhesion complex on the plasma membrane.
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