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STIP1 is an adaptor protein that coordinates the functions of HSP70 (see HSPA1A\; MIM 140550) and HSP90 (see HSP90AA1\; MIM 140571) in protein folding.
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In conclusion, STIP1 is upregulated in HCC (show FAM126A Proteins) and associated with poor clinical prognosis. Blocking STIP1 activity suppresses HCC (show FAM126A Proteins) cell growth, providing the rationale for STIP1 as a potential therapeutic target in HCC (show FAM126A Proteins).
Domains of STIP1 responsible for regulating PrPC (show PRNP Proteins)-dependent amyloid-beta oligomer toxicity
Reduced STIP1 levels can contribute to phenotypes related to hyperactivity and attention deficits.
We correlate the expression of STI1 and glioma progression, and suggest that STI1 expression in microglia/macrophages and infiltrating lymphocytes is modulated by the brain tumor microenvironment.
Knockdown of PIAS1 (show PIAS1 Proteins) in astrocytes impairs the accumulation of nuclear STI1 in response to irradiation. Moreover, a PIAS1 (show PIAS1 Proteins) mutant lacking the STI1 binding site is unable to increase STI1 nuclear retention.
stress-inducible protein-1 has a role in recruitment of bone marrow derived cells into the ischemic brains
Our findings reveal a previously unrecognized role of the PrP(C (show PRNP Proteins)) ligand STI1 in protecting neurons in Alzheimer disease and suggest a novel pathway that may help to offset AbetaO-induced toxicity.
Stress-inducible phosphoprotein 1 has unique cochaperone activity during development and regulates cellular response to ischemia via the prion protein (show PRNP Proteins).
STI1 and laminin-gamma1 promote robust axonogenesis in wild-type dorsal root ganglia neurons; STI1 promotes extracellular calcium influx.
Neuroprotection and neuritogenesis mediated by PrP(C (show PRNP Proteins))-STI1 engagement are dependent upon the increased protein synthesis mediated by PI3K-mTOR (show FRAP1 Proteins) signaling.
Functional studies showed that STIP1 promoted the growth, colony formation and migration of cancer cells. However, knocking down the expression of STIP1 inhibited the growth, colony formation and migration of cancer cells.
In vitro experiments revealed that STIP1 was capable of binding to the MMP-9 (show MMP9 Proteins) promoter and enhanced its transcriptional expression
STIP1 modulates the function of the HSP90 (show HSP90 Proteins)-JAK2 (show JAK2 Proteins)-STAT3 (show STAT3 Proteins) complex
Hsp70/Hsp90-organizing protein promoter activity was highest in Hs578T which expressed mutant or inactive p53 (show TP53 Proteins). HRAS (show HRAS Proteins) activation of the Hsp70/Hsp90-organizing protein promoter was inhibited by p53 (show TP53 Proteins) overexpression.
the modulation of HOP-PrP(C (show PRNP Proteins)) engagement or the decrease of PrP(C (show PRNP Proteins)) and HOP expression may represent a potential therapeutic intervention in glioblastoma.
Data suggest that calcium signaling plays important role in prevention of protein misfolding; complexes of S100A1 (show S100A1 Proteins) and STIP1 are key players in this pathway; the stoichiometry of S100A1 (show S100A1 Proteins)/STIP1 interaction appears to be three S100A1 (show S100A1 Proteins) dimers plus one STIP1 monomer; each S100A1 (show S100A1 Proteins)-STIP1-binding interaction is entropically driven. (S100A1 (show S100A1 Proteins) = S100 calcium binding protein A1 (show S100A1 Proteins); STIP1 = stress-induced-phosphoprotein 1) [REVIEW]
Results indicte the great potential of STIP1 (stress-induced phosphoprotein 1) as a biomarker and therapeutic target in renal cell carcinoma (show MOK Proteins) (RCC (show XRCC1 Proteins)) bone metastasis.
Data suggest that three dimers of S100A1 (S100 calcium binding protein A1 (show S100A1 Proteins)) associate with one molecule of STIP1 (stress-inducible phosphoprotein 1) in a calcium-dependent manner; individual STIP1 TPR (tetratricopeptide repeat) domains, TPR1, TPR2A and TPR2B, bind a single S100A1 (show S100A1 Proteins) dimer with significantly different affinities; TPR2B domain possesses highest affinity for S100A1 (show S100A1 Proteins).
Data confirmed the significant up-regulation of STIP1 in tumorous cholangiocytes relative to normal hepatocytes and non-tumorous cells and show prooved it as a reliable diagnostic biomarker when using immunohistochemistry.
STIP1 is an adaptor protein that coordinates the functions of HSP70 (see HSPA1A\; MIM 140550) and HSP90 (see HSP90AA1\; MIM 140571) in protein folding. It is thought to assist in the transfer of proteins from HSP70 to HSP90 by binding both HSP90 and substrate-bound HSP70. STIP1 also stimulates the ATPase activity of HSP70 and inhibits the ATPase activity of HSP90, suggesting that it regulates both the conformations and ATPase cycles of these chaperones (Song and Masison, 2005
, stress-induced-phosphoprotein 1 (Hsp70/Hsp90-organizing protein)
, Stress-induced-phosphoprotein 1
, Hsp70/Hsp90 organizing protein
, IEF SSP 3521
, hsc70/Hsp90-organizing protein
, stress-inducible protein
, Hsc70/Hsp90-organizing protein
, Hsp70/Hsp90-organizing protein
, NY-REN-11 antigen
, renal carcinoma antigen NY-REN-11
, transformation-sensitive protein IEF SSP 3521
, septin and tuftelin-interacting protein 1
, tuftelin-interacting protein 11