Interactions of the Protein-tyrosine Phosphatase-α with the Focal Adhesion Targeting Domain of Focal Adhesion Kinase Are Involved in Interleukin-1 Signaling in Fibroblasts [PDF]
Interleukin-1 (IL-1) signaling in fibroblasts is mediated through focal adhesions, organelles that are enriched with adaptor and cytoskeletal proteins that regulate signal transduction. We examined interactions of the focal adhesion kinase (FAK) with protein-tyrosine phosphatase-α (PTP-α) in IL-1 signaling.
Qin Wang +5 more
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A role for the protein tyrosine phosphatase CD45 in macrophage adhesion through the regulation of paxillin degradation. [PDF]
CD45 is a protein tyrosine phosphatase expressed on all cells of hematopoietic origin that is known to regulate Src family kinases. In macrophages, the absence of CD45 has been linked to defects in adhesion, however the molecular mechanisms involved ...
Joëlle St-Pierre, Hanne L Ostergaard
doaj +2 more sources
Protein tyrosine phosphatase 1B targets focal adhesion kinase and paxillin in cell–matrix adhesions [PDF]
ABSTRACT Protein tyrosine phosphatase 1B (PTP1B, also known as PTPN1) is an established regulator of cell-matrix adhesion and motility. However, the nature of substrate targets at adhesion sites remains to be validated. Here, we used bimolecular fluorescence complementation assays, in combination with a substrate trapping mutant of PTP1B,
Ana E. González Wusener +5 more
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Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. [PDF]
A homology-based cDNA cloning approach was used to identify a widely expressed protein-tyrosine kinase designated as "focal adhesion kinase" (FadK). The entire mouse FadK amino acid sequence was deduced from cDNA clones, revealing a large (119-kDa) non-membrane-spanning protein-tyrosine kinase that lacks Src-homology SH2 and SH3 domains. Immunostaining
Steven K. Hanks +3 more
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Activation of p38 Mitogen-activated Protein Kinase by PYK2/Related Adhesion Focal Tyrosine Kinase-dependent Mechanism [PDF]
The stress-activated p38 mitogen-activated protein kinase (p38 MAPK), a member of the subgroup of mammalian kinases, appears to play an important role in regulating inflammatory responses, including cytokine secretion and apoptosis.
Pramod S. Pandey +11 more
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Phosphorylation of p130Cas initiates Rac activation and membrane ruffling [PDF]
Background Non-receptor tyrosine kinases (NTKs) regulate physiological processes such as cell migration, differentiation, proliferation, and survival by interacting with and phosphorylating a large number of substrates simultaneously.
Sharma Alok, Mayer Bruce J
doaj +3 more sources
Grb2 Promotes Integrin-Induced Focal Adhesion Kinase (FAK) Autophosphorylation and Directs the Phosphorylation of Protein Tyrosine Phosphatase α by the Src-FAK Kinase Complex [PDF]
The integrin-activated Src-focal adhesion kinase (FAK) kinase complex phosphorylates PTPα at Tyr789, initiating PTPα-mediated signaling that promotes cell migration. Recruitment of the BCAR3-Cas complex by PTPα-phospho-Tyr789 at focal adhesions is one mechanism of PTPα signaling.
Suzanne Y. S. Cheng +3 more
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Rapid Tyrosine Phosphorylation of Neuronal Proteins Including Tau and Focal Adhesion Kinase in Response to Amyloid-β Peptide Exposure: Involvement of Src Family Protein Kinases [PDF]
The increased production of amyloid β-peptide (Aβ) in Alzheimer's disease is acknowledged to be a key pathogenic event. In this study, we examined the response of primary human and rat brain cortical cultures to Aβ administration and found a marked ...
Ritchie Williamson +10 more
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Autonomous Expression of a Noncatalytic Domain of the Focal Adhesion-Associated Protein Tyrosine Kinase pp125FAK [PDF]
Integrins play a central role in cellular adhesion and anchorage of the cytoskeleton and participate in the generation of intracellular signals, including tyrosine phosphorylation. We have recently isolated a cDNA encoding a unique, focal adhesion-associated protein tyrosine kinase (FAK) that is a component of an integrin-mediated signal transduction ...
Michael D. Schaller +2 more
openalex +4 more sources
Phosphorylated α-Actinin and Protein-tyrosine Phosphatase 1B Coregulate the Disassembly of the Focal Adhesion Kinase·Src Complex and Promote Cell Migration* [PDF]
The focal adhesion kinase (FAK) is a key regulator of cell migration. Phosphorylation at Tyr-397 activates FAK and creates a binding site for Src family kinases. FAK phosphorylates the cytoskeletal protein α-actinin at Tyr-12. Here we report that protein-
Zhiyong Zhang +3 more
semanticscholar +3 more sources

