Paxillin and focal adhesion signalling

By C. Turner. Nature Cell Biology, 2000

850 citations recorded by the source corpus.

Subfields: Cell Biology, Immunology and Allergy, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/3fe185cf2325680291d7e3783400db5c967b200a

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. David M. Sabatini
2. D. Hocking
3. J. Sottile
4. K. Legate
5. J. Parsons
6. P. Keely
7. R. Fässler
8. S. Wickström

In Immunology and Allergy

1. D. Hocking
2. J. Sottile
3. K. Legate
4. J. Parsons
5. P. Keely
6. R. Fässler
7. S. Wickström
8. R. Zent

In Molecular Biology

1. David M. Sabatini
2. D. Guertin
3. M. Laplante
4. Siraj M. Ali
5. Dos D. Sarbassov
6. Paul Tempst
7. H. Erdjument‐Bromage
8. Michael N. Hall

Citations in the corpus

• Focal adhesion regulation of cell behavior. (2004, background): “…has a proline-rich motif that binds to the Src SH3 domain, five LD motifs that are responsible for its interactions with several proteins including FAK and PKL, as well as four C-terminal LIM domains with which paxillin attaches to the cell membrane and interacts with the phosphatase PTP-PEST [73].”
• Focal adhesion kinase: the first ten years (2003, background): “Data support a model by which Cdc42/Rac activation of PAK stimulates the binding of PAK to PIX, which in turn induces binding of PAK-PIX to PKL-paxillin (Brown et al., 2002; Turner, 2000a).”
• Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions. (2002, background): “Integrin ligation leads to clustering of integrins into focal contacts, areas of the cell that are in close apposition to the substrate (Izzard and Lochner, 1980; Chen and Singer, 1982), and that are rich in signaling and cytoskeletal proteins, including FAK, paxillin, and vinculin (Singer, 1982; Pa”
• Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. (2004, background): “The morphology of the actin cytoskeleton in cells with siRNA-mediated reductions in PKC (cid:6) is similar but between the actin cytoskeleton and the plasma membrane [21], is also altered in the rictor and mTOR knock-not a mimic of that in the rictor knockdown cells.”
• Genetic and cell biological analysis of integrin outside-in signaling. (2009, background): “…is tyrosine-phosphorylated by Src and FA kinase (FAK) (Bellis et al. 1995; Schaller and Parsons 1995), which creates a binding site for Crk (Turner 2000). p130 Crk-associated substrate (p130Cas) can be phosphorylated within FAs in response to mechanical stretch, which in turn creates…”
• α4β1- and α6β1-integrins are functional receptors for midkine, a heparin-binding growth factor (2004, background): “We also found that, in UMR-106 osteoblastic cells, soluble MK transiently increased the tyrosine phosphorylation of paxillin, which is an adapter molecule that directly binds to the cytoplasmic portion of α4-integrins (Turner, 2000; Schaller, 2001; Rose et al., 2002).”
• Integrin Structure and Function (2010, background): “Paxillin is a structural protein that allows numerous simultaneous interactions, which are further modified by phosphorylation (Turner 2000).”