@article{Klingbeil2001Targe-8752,
  year={2001},
  doi={10.1083/jcb.152.1.97},
  title={Targeting Pyk2 to Beta1-Integrin containing Focal Contacts Rescues Fibronectin stimulated Signaling and Haptotactic Motility Defects of Focal Adhesion Kinase null Cells},
  number={1},
  volume={152},
  issn={0021-9525},
  journal={Journal of Cell Biology},
  pages={97--110},
  author={Klingbeil, Candice K. and Hauck, Christof R. and Hsia, Datsun A. and Reider, Shannon R. and Jones, K. C. and Schlaepfer, David D.}
}

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    <dc:contributor>Klingbeil, Candice K.</dc:contributor>
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    <dc:contributor>Hsia, Datsun A.</dc:contributor>
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    <dc:creator>Reider, Shannon R.</dc:creator>
    <dc:creator>Hauck, Christof R.</dc:creator>
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    <dcterms:abstract xml:lang="eng">Focal adhesion kinase null (FAK-/-) fibroblasts exhibit morphological and motility defects that are reversed by focal adhesion kinase (FAK) reexpression. The FAK-related kinase, proline-rich tyrosine kinase 2 (Pyk2), is expressed in FAK-/- cells, yet it exhibits a perinuclear distribution and does not functionally substitute for FAK. Chimeric Pyk2/FAK proteins were created and expressed in FAK-/- cells to determine the impact of Pyk2 localization to focal contacts. Whereas an FAK/Pyk2 COOH-terminal (CT) domain chimera was perinuclear distributed, stable expression of a Pyk2 chimera with the FAK-CT domain (Pyk2/FAK-CT) localized to focal contact sites and enhanced fibronectin (FN)-stimulated haptotactic cell migration equal to FAK-reconstituted cells. Disruption of paxillin binding to the FAK-CT domain (S-1034) inhibited Pyk2/FAK-CT localization to focal contacts and its capacity to promote cell motility. Paxillin binding to the FAK-CT was necessary but not sufficient to mediate the indirect association of FAK or Pyk2/FAK-CT with a ß1-integrin containing complex. Both FAK and Pyk2/FAK-CT but not Pyk2/FAK-CT S-1034 reconstituted FAK-/- cells, exhibit elevated FN-stimulated extracellular signal regulated kinase 2 (ERK2) and c-Jun NH2-terminal kinase (JNK) kinase activation. FN-stimulated FAK or Pyk2/FAK-CT activation enhanced both the extent and duration of FN-stimulated ERK2 activity which was necessary for cell motility. Transient overexpression of the FAK-CT but not FAK-CT S-1034 domain inhibited both FN-stimulated ERK2 and JNK activation as well as FN-stimulated motility of Pyk2/FAK-CT reconstituted cells. These gain-of-function studies show that the NH2-terminal and kinase domains of Pyk2 can functionally substitute for FAK in promoting FN-stimulated signaling and motility events when localized to ß-integrin containing focal contact sites via interactions mediated by the FAK-CT domain.</dcterms:abstract>
    <dc:contributor>Schlaepfer, David D.</dc:contributor>
    <dc:contributor>Hauck, Christof R.</dc:contributor>
    <dcterms:bibliographicCitation>First publ. in: Journal of Cell Biology 152 (2001), 1, pp. 97 110</dcterms:bibliographicCitation>
    <dc:creator>Schlaepfer, David D.</dc:creator>
    <dcterms:title>Targeting Pyk2 to Beta1-Integrin containing Focal Contacts Rescues Fibronectin stimulated Signaling and Haptotactic Motility Defects of Focal Adhesion Kinase null Cells</dcterms:title>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:46:12Z</dc:date>
    <dc:creator>Jones, K. C.</dc:creator>
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    <dc:creator>Hsia, Datsun A.</dc:creator>
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