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TRIP6 promotes tumor proliferation and reverses cell adhesion-mediated drug resistance via regulating nuclear p27(Kip1 (show CDKN1B Proteins)) 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 (show CDKN1B Proteins)) 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 (show APOA Proteins)) and NF-kappaB (show NFKB1 Proteins) signaling.
TRIP6 is an adaptor protein that regulates cell motility, antiapoptotic signaling and transcriptional activity. (Review)
TRIP6 promotes Fas (show FAS Proteins)-mediated cell migration in apoptosis-resistant glioma cells. This effect is regulated via the Src (show SRC Proteins)-dependent phosphorylation of TRIP6 at Tyr (show TYR Proteins)-55.
the OIP-1 c-peptide is the functional domain of OIP-1
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
TRIP6 functions at a point of convergence between the activated LPA(2 (show LPAR2 Proteins)) receptor and downstream signals involved in cell adhesion and migration
TRIP6 in lysophosphatidic acid signaling is regulated by c-Src (show SRC Proteins)-mediated phosphorylation of TRIP6 at the Tyr (show TYR Proteins)-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