Christopher E. Turner

Molecular dissection of actopaxin-integrin-linked kinase-Paxillin interactions and their role in subcellular localization.

The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling.

The paxillin LD motifs.

A fragment of paxillin binds the alpha 4 integrin cytoplasmic domain (tail) and selectively inhibits alpha 4-mediated cell migration.

Epidermal growth factor stimulates serine/threonine phosphorylation of the focal adhesion protein paxillin in a MEK-dependent manner in normal rat kidney cells.

Actopaxin is phosphorylated during mitosis and is a substrate for cyclin B1/cdc2 kinase.

Roles for the tubulin- and PTP-PEST-binding paxillin LIM domains in cell adhesion and motility.

Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathway.

Ca2+-dependent localization of integrin-linked kinase to cell junctions in differentiating keratinocytes.

Extracellular signal-regulated kinase mediates phosphorylation of tropomyosin-1 to promote cytoskeleton remodeling in response to oxidative stress: impact on membrane blebbing.

Crk associates with a multimolecular Paxillin/GIT2/beta-PIX complex and promotes Rac-dependent relocalization of Paxillin to focal contacts.

RNF5, a RING finger protein that regulates cell motility by targeting paxillin ubiquitination and altered localization.

Expression of non-phosphorylatable paxillin mutants in canine tracheal smooth muscle inhibits tension development.

Tension development during contractile stimulation of smooth muscle requires recruitment of paxillin and vinculin to the membrane.

FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly.

Integrin-linked kinase: a possible role in scar contracture.

EphB1-mediated cell migration requires the phosphorylation of paxillin at Tyr-31/Tyr-118.

Vinculin modulation of paxillin-FAK interactions regulates ERK to control survival and motility.

Phosphorylation of actopaxin regulates cell spreading and migration.

Paxillin: adapting to change.

The integrin-linked kinase regulates cell morphology and motility in a rho-associated kinase-dependent manner.

Actopaxin interacts with TESK1 to regulate cell spreading on fibronectin.

Src and FAK kinases cooperate to phosphorylate paxillin kinase linker, stimulate its focal adhesion localization, and regulate cell spreading and protrusiveness.

Tyrosine-phosphorylated Hic-5 inhibits epidermal growth factor-induced lamellipodia formation.

Regulation of paxillin family members during epithelial-mesenchymal transformation: a putative role for paxillin delta.

Paxillin is essential for PTP-PEST-dependent regulation of cell spreading and motility: a role for paxillin kinase linker.

CdGAP associates with actopaxin to regulate integrin-dependent changes in cell morphology and motility.

Hic-5 contributes to epithelial-mesenchymal transformation through a RhoA/ROCK-dependent pathway.

TGF-beta1 slows the growth of pathogenic myofibroblasts through a mechanism requiring the focal adhesion protein, Hic-5.

Paxillin-dependent stimulation of microtubule catastrophes at focal adhesion sites.

Hic-5 promotes the hypertrophic scar myofibroblast phenotype by regulating the TGF-beta1 autocrine loop.

Paxillin comes of age.

Cross talk between paxillin and Rac is critical for mediation of barrier-protective effects by oxidized phospholipids.

FAK engages multiple pathways to maintain survival of fibroblasts and epithelia: differential roles for paxillin and p130Cas.

Paxillin-kinase-linker tyrosine phosphorylation regulates directional cell migration.

Emerging role of paxillin-PKL in regulation of cell adhesion, polarity and migration.

The cell adhesion-associated protein Git2 regulates morphogenetic movements during zebrafish embryonic development.

Distinct roles for paxillin and Hic-5 in regulating breast cancer cell morphology, invasion, and metastasis.

LNK (SH2B3) is a key regulator of integrin signaling in endothelial cells and targets α-parvin to control cell adhesion and migration.

Hic-5 promotes invadopodia formation and invasion during TGF-β-induced epithelial-mesenchymal transition.

Paxillin and Hic-5 interaction with vinculin is differentially regulated by Rac1 and RhoA.

CdGAP regulates cell migration and adhesion dynamics in two-and three-dimensional matrix environments.

Actopaxin (α-parvin) phosphorylation is required for matrix degradation and cancer cell invasion.

Beta2-adaptin binds actopaxin and regulates cell spreading, migration and matrix degradation.

Diverse roles for the paxillin family of proteins in cancer.

Paxillin kinase linker (PKL) regulates Vav2 signaling during cell spreading and migration.

LIM domains target actin regulators paxillin and zyxin to sites of stress fiber strain.

The focal adhesion-localized CdGAP regulates matrix rigidity sensing and durotaxis.

Paxillin inhibits HDAC6 to regulate microtubule acetylation, Golgi structure, and polarized migration.