Tensin 3 is a new partner of Dock5 that controls osteoclast podosome organization and activity
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Title
Tensin 3 is a new partner of Dock5 that controls osteoclast podosome organization and activity
Authors
Keywords
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Journal
JOURNAL OF CELL SCIENCE
Volume 129, Issue 18, Pages 3449-3461
Publisher
The Company of Biologists
Online
2016-08-04
DOI
10.1242/jcs.184622
References
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Related references
Note: Only part of the references are listed.- Tensin1 positively regulates RhoA activity through its interaction with DLC1
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- A phosphorylation switch controls the spatiotemporal activation of Rho GTPases in directional cell migration
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- The mineral dissolution function of osteoclasts is dispensable for hypertrophic cartilage degradation during long bone development and growth
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- Dock-family exchange factors in cell migration and disease
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- Differential regulation of the activity of deleted in liver cancer 1 (DLC1) by tensins controls cell migration and transformation
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- Rac deletion in osteoclasts causes severe osteopetrosis
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- The Tensin-3 Protein, Including its SH2 Domain, Is Phosphorylated by Src and Contributes to Tumorigenesis and Metastasis
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- Podosome-like structures of non-invasive carcinoma cells are replaced in epithelial-mesenchymal transition by actin comet-embedded invadopodia
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- Rho GTPases in osteoclasts: Orchestrators of podosome arrangement
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- An α-Helical Extension of the ELMO1 Pleckstrin Homology Domain Mediates Direct Interaction to DOCK180 and Is Critical in Rac Signaling
- (2008) David Komander et al. MOLECULAR BIOLOGY OF THE CELL
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