NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model (Q27642755)

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English	NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model	scientific article

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scholarly article

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NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model (English)

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solution structure

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based on heuristic

inferred from title

author name string

Guanghua Gao

1

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Kirk C Prutzman

2

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Michelle L King

3

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Danielle M Scheswohl

4

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Eugene F DeRose

5

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Robert E London

6

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Michael D Schaller

7

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Sharon L Campbell

8

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language of work or name

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publication date

27 February 2004

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Journal of Biological Chemistry

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279

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9

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8441-51

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Signaling through focal adhesion kinase

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Focal adhesion kinase mediates the integrin signaling requirement for growth factor activation of MAP kinase

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Differential regulation of cell motility and invasion by FAK

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Control of adhesion-dependent cell survival by focal adhesion kinase

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Bombesin and gastrin releasing peptide increase tyrosine phosphorylation of focal adhesion kinase and paxillin in non-small cell lung cancer cells

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Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase

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Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions

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Interaction of focal adhesion kinase with cytoskeletal protein talin

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Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK

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Paxillin binding is not the sole determinant of focal adhesion localization or dominant-negative activity of focal adhesion kinase/focal adhesion kinase-related nonkinase

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Focal adhesion targeting: the critical determinant of FAK regulation and substrate phosphorylation

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A mechanism for regulation of the adhesion-associated proteintyrosine kinase pp125FAK.

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Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses

1 reference

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Paxillin binding to the alpha 4 integrin subunit stimulates LFA-1 (integrin alpha L beta 2)-dependent T cell migration by augmenting the activation of focal adhesion kinase/proline-rich tyrosine kinase-2.

1 reference

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Paxillin alpha and Crk-associated substrate exert opposing effects on cell migration and contact inhibition of growth through tyrosine phosphorylation

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Phosphorylation of tyrosine residues 31 and 118 on paxillin regulates cell migration through an association with CRK in NBT-II cells

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The role of focal adhesion kinase binding in the regulation of tyrosine phosphorylation of paxillin

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Paxillin: a focal adhesion-associated adaptor protein

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Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding

1 reference

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The paxillin LD motifs

1 reference

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The structural basis of localization and signaling by the focal adhesion targeting domain

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The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin

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Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase

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TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe.

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pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions

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Identifiers

10.1074/JBC.M309808200

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release_qxipfvbodvdebmmabjqn7irmh4

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