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TRIP6 acts as an intermediary connecting tension monitoring at adherens junctions to Hippo signaling, which has implications for how tension contributes to growth of organs and tissues during development, tissue repair during injury and to pathological conditions such as cancer.
Taken together, these findings showed that TRIP6 plays an important role in promoting HCC cells proliferation and may serve as a novel prognostic biomarker and therapeutic target in HCC.
TRIP6 promotes tumor proliferation and reverses cell adhesion-mediated drug resistance via regulating nuclear p27(Kip1) expression in non-Hodgkin's lymphoma
the Trip6-GRIP1-myosin VI interaction and its regulation on F-actin network play a significant role in dendritic morphogenesis
TRIP6 overexpression promotes migration, invasion, and clonogenicity of Ewing's sarcoma cells
TRIP6 is involved in the regulation of nasopharyngeal carcinoma cell motility, and phosphorylation of tyrosine 55 residue plays an important regulatory role for this event
TRIP6 also promotes serum-induced reduction of nuclear p27(KIP1) expression levels.
High TRIP6 expression is associated with malignant pleural mesothelioma.
TRIP6 is a nucleocytoplasmatic shuttle protein essential for the coordination of focal adhesion dynamics and transcriptional responses in lysophosphosphatidic (LPA) and NF-kappaB signaling.
TRIP6 is an adaptor protein that regulates cell motility, antiapoptotic signaling and transcriptional activity. (Review)
TRIP6 promotes Fas-mediated cell migration in apoptosis-resistant glioma cells. This effect is regulated via the Src-dependent phosphorylation of TRIP6 at Tyr-55.
the OIP-1 c-peptide is the functional domain of OIP-1
TRIP6 functions at a point of convergence between the activated LPA(2) receptor and downstream signals involved in cell adhesion and migration
ZRP-1 has a role in endoglin regulation of cytoskeletal organization
The data establish a physical and functional association between TRIP6 and RIP2, and suggest that RIP2's involvement in multiple NF-kappaB and ERK activation pathways is mediated through TRIP6.
Binding of LPP and TRIP6 to Scrib links Scrib to a communication pathway between cell-cell contacts and the nucleus, and implicates these zyxin family members in Scrib-associated functions.
The TRIP6 knock-down led to an increased number of longer stress fibers and to the induction of locomotive phenotype in carcinoma cells.
AMPK phosphorylated TRIP6 in vitro at the N-terminus and the transcriptional co-activator properties of TRIP6 were enhanced by AMPK action.
Data report that nTRIP6 acts as a co-repressor for MEF2C in myoblasts. nTRIP6 interacts via its N-terminal pre-LIM region with MEF2C in the nucleus of myoblasts, is recruited together with MEF2C to the regulatory regions of MEF2C target genes and represses their expression.
Our data suggest that TRIP6 regulates neural stem cell maintenance and it may be a new marker for neural stem cells.
Data show that OIP-1 (Trip6) is an important physiologic regulator of osteoclast development and may have therapeutic utility for bone diseases with high bone turnover.
TRIP6 is a critical downstream regulator of c-Src signaling and its phosphorylation is permissive for its presence in the sealing zone where it plays a positive role in osteoclast bone resorptive capacity
nTrip6 serves as the molecular mediator of the crosstalk between nuclear receptors and other transcription factors in that it assembles these factors at promoters.
TRIP6 in lysophosphatidic acid signaling is regulated by c-Src-mediated phosphorylation of TRIP6 at the Tyr-55 residue.
nTrip6 interacts only with Fos family members. Consequently, nTrip6 is a selective coactivator for AP-1 dimers containing Fos. nTrip6 also assembles activated GR to c-Jun:c-Fos-driven promoters.
This gene is a member of the zyxin family and encodes a protein with three LIM zinc-binding domains. This protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner and it regulates LPA-induced cell migration. Alternatively spliced variants which encode different protein isoforms have been described\; however, not all variants have been fully characterized.
thyroid hormone receptor interactor 6
, thyroid receptor-interacting protein 6-like
, thyroid receptor-interacting protein 6
, OPA-interacting protein 1
, TR-interacting protein 6
, thyroid hormone receptor interacting protein 6
, zyxin related protein 1
, zyxin-related protein 1