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Focal adhesions are actin-rich structures that enable cells to adhere to the extracellular matrix and at which protein complexes involved in signal transduction assemble.
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ZYX-1 is a conserved LIM (show PDLIM5 Proteins) domain-containing focal adhesion protein that regulates synapse maintenance in Caenorhabditis elegans
The zyx-1 gene encodes two different isoforms, ZYX-1a and ZYX-1b, which exhibit different roles in dystrophin (show DMD Proteins)-dependent muscle degeneration in C. elegans
DYC-1 interacts with ZYX-1, the homologue of the vertebrate focal adhesion LIM domain protein (show PDLIM7 Proteins) zyxin.
results show that Zyxin is a functional antagonist of Expanded in growth control
The motor domain of DmMyo20 could specifically bind to actin (show ACTB Proteins) filaments in an ATP-independent manner and enhance the interaction between actin (show ACTB Proteins) filaments and Zyx102, a downstream component of DmMyo20 in the Fat signaling pathway.
Through epistasis tests, the requirement for Zyx is positioned within the Fat branch of Hippo signaling, downstream of Fat and Dco (show CSNK1E Proteins), and upstream of the Yorkie (show YAP1 Proteins) kinase Warts.
Reduction of Zyx102 protein levels using RNA-interference results in lethality at the pharate adult stage.
Increased zyxin expression is associated with asthma.
VASP (show VASP Proteins), zyxin and TES (show TES Proteins) are tension-dependent members of focal adherens junctions independent of the alpha-catenin (show CTNNA1 Proteins)-vinculin (show VCL Proteins) module.
Zyxin binding to Ptc2 (show PTCH2 Proteins) is due to the interaction of Zyxin 2nd LIM (show PDLIM5 Proteins)-domain (530-590 aa) with the under-membrane region of the cytoplasmic C-terminus of Ptc2 (show PTCH2 Proteins) (1159-1412 aa).
ZYX gene may be aging-related gene and involved in Osteoporosis.
Matrix density alters zyxin phosphorylation, which limits peripheral process formation and extension in endothelial cells invading 3D collagen matrices.
Zyxin, which is thought to be essential for tight cell-to-cell junctions, decreased 1.8-fold in TNF-alpha (show TNF Proteins)-treated human brain microvascular endothelial cells.
Integrin-beta5 and zyxin mediate formation of ventral stress fibers in response to transforming growth factor beta.
Zyxin is a novel target for beta-amyloid peptide (show APP Proteins) activities in Alzheimer's disease.
Zyxin is suggested to promote growth, migration and invasiveness of fibroblastic type oral squamous cell carcinoma cells by upregulating Rac1 and Cdc42 (show CDC42 Proteins).
A stretch-induced signaling pathway in vascular cells leads to the activation of zyxin, a cytoskeletal protein (show ACTN1 Proteins) specifically involved in transducing mechanical stimuli.
zyxin influences focal adhesion dynamics, that it recruits Tes (show TES Proteins) and that this interaction is functional in regulating cell spreading.
Zyxin contributes to the migratory and invasive phenotype evoked by Tead2 (show TEAD2 Proteins).
paxillin (show PXN Proteins) and zyxin are LIM (show PDLIM5 Proteins)-domain adaptor proteins that are recruited to stress fiber strain sites
Zyxin regulates migration of renal epithelial cells through activation of hepatocyte nuclear factor-1beta.
Zyxin is a transforming growth factor-beta (TGF-beta)/Smad3 (show SMAD3 Proteins) target gene that regulates lung cancer cell motility via integrin alpha5beta1.
a bipartite mechanism for stretch-induced actin remodeling involves mechanosensitive targeting of zyxin to actin stress fibers and localized recruitment of actin regulatory machinery
Mice that lack zyxin function are viable and fertile and display no obvious histological abnormalities in any of the organs examined.Specifically, we evaluated blood platelet function, nervous system development, and skin architecture
LIM-nebulette (show NEBL Proteins), Lasp-1 (show LASP1 Proteins), and zyxin may play an important role in the organization of focal adhesions
Cooperates with Ena, vasodilator-stimulated phosphoprotein, and caldesmon to influence integrin-dependent cell motility and actin stress fiber remodeling.
Zyxin inhibits Shh (show SHH Proteins) signaling during the CNS patterning in Xenopus laevis through interaction with Gli1 (show GLI1 Proteins)
These results are consistent with a possible role of Zyxin as a negative modulator of Xanf1 transcriptional repressing activity.
binding of the LIM2 domain of zyxin with the Engrailed Homology 1 repressor domain of Xanf1 is responsible for the interaction of these proteins.
Focal adhesions are actin-rich structures that enable cells to adhere to the extracellular matrix and at which protein complexes involved in signal transduction assemble. Zyxin is a zinc-binding phosphoprotein that concentrates at focal adhesions and along the actin cytoskeleton. Zyxin has an N-terminal proline-rich domain and three LIM domains in its C-terminal half. The proline-rich domain may interact with SH3 domains of proteins involved in signal transduction pathways while the LIM domains are likely involved in protein-protein binding. Zyxin may function as a messenger in the signal transduction pathway that mediates adhesion-stimulated changes in gene expression and may modulate the cytoskeletal organization of actin bundles. Alternative splicing results in multiple transcript variants that encode the same isoform.
ZYXin family member (zyx-1)
, hypothetical protein LOC779718