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HIP1 gene expression might serve as a reliable predictor for overall survival in acute myeloid leukemia patients.
After HIP1 expression was blocked by siRNAs, EGFR endocytosis was accelerated and this effect was dependent on the EGF concentration. This endocytosis was colocalized with clathrin expression. These findings indicate that the inhibition of HIP1 can accelerate the endocytosis and degradation of EGFR
Data suggest that GLP1R signaling in pancreatic beta-cells leading to insulin secretion involves interactions of GLP1R with HIP1, SNX1, and SNX27; HIP1 appears to regulate coupling of cell surface GLP1R activation with endocytosis; SNX1 and SNX27 appear to control balance between GLP1R plasma membrane recycling and lysosomal degradation.
HIP1 deletion is not involved in Williams-Beuren syndrome.
Huntingtin-interacting protein-1 (HIP1) is known to play a role in tumorigenesis. metastasis. Read More: http://www.atsjournals.org/doi/full/10.1164/rccm.201412-2226OC#.V8DF69LrtNs
SHON is a novel human oncogene with predictive utility in ER(+) breast cancer, perhaps offering a simple biomarker to predict the therapeutic efficacy of antiestrogen therapy in patients with breast cancer.
SHON plays an important role in EMT and contributes to breast cancer progression.
HIP1-ALK, a novel fusion protein is associated with lung adenocarcinoma.
HIP1-ALK-rearranged tumor is sensitive to treatment with crizotinib, implicating HIP1-ALKas an oncogenic driver of lung tumorigenesis
Identified a four-tyrosine "HIP1 phosphorylation motif" in the N-terminal region of HIP1 that is required for phosphorylation mediated by both EGFR and PDGFbetaR but not by the oncoproteins HIP1/PDGFbetaR (H/P), and TEL/PDGFbetaR (T/P).
Three neuronal proteins (Huntingtin interacting protein 1, neurofascin, and olfactomedin-like 2a) are novel components of podocyte major processes and their expression in glomerular crescents supports their role in crescent formation.
flexibility of the HIP1 coiled-coil domain is important for normal function and may lead to new insights into Huntington's disease
A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.
Huntingtin-interacting protein 1 is a Merkel cell carcinoma marker that interacts with c-Kit
data characterize a neurodevelopmental and epilepsy syndrome that is likely caused by recurrent and nonrecurrent deletions, including HIP1
hydrogen-bond network and changes in coiled-coil monomer interaction suggest that the HIP1 coiled-coil domain is uniquely suited to allow conformational flexibility.
Results show that pro-apoptotic Hippi-Hip-1 heterodimers can recruit procaspase-8 into a complex of Hippi, Hip-1 and procaspase-8, and launch apoptosis through components of the 'extrinsic' cell-death pathway.
HIP1 and HIP12 display differential binding to F-actin, AP2, and clathrin. Identification of a novel interaction with clathrin light chain.
huntingtin-interacting protein 1 is overexpressed in prostate and colon cancer and is critical for cellular survival
both HIP1r and HIP1 bind inositol lipids via their epsin N-terminal homology (ENTH) domains.
Huntingtin-interacting protein 1 (Hip1) functions in Notch-mediated neurogenesis and provides a functional link between Notch signaling and proteins related to Huntington disease.
we show that M. tuberculosis impairs dendritic cell cytokine secretion, maturation, and antigen presentation through the cell envelope-associated serine hydrolase, Hip1.
HIP1 association with and phosphorylation mediated by EGFR and EGFRvIII.
Results show that pro-apoptotic Hippi-Hip-1 heterodimers can recruit procaspase-8 into a complex of Hippi, Hip-1 and procaspase-8, and launch apoptosis through components of the 'extrinsic' cell-death pathw
HIP1 is the first endocytic protein to be directly implicated in tumor formation
disuprtion results in neurological deficits and decreased AMPA receptor trafficking
three different mutations lead to hematopoietic abnormalities reflected by diminished early progenitor frequencies
mice deficient in both HIP1 and HIP1r have accelerated development of abnormalities seen in Hip1 -deficient mice, including kypholordosis and growth defects
The various abnormalities corroborate reduced fertility levels in HIP1(-/-) mice and suggest a role for HIP1 in stabilizing actin and microtubules, enabling normal spermatid and Sertoli cell morphology and function.
we have shown that HIP1 influences important NMDAR functions and that both HIP1 and htt participate in NMDA-induced cell death.
Degenerative phenotypes seen in knockout mice are due mainly to HIP1 and HIP1r protein deficiency rather than altered expression of neighboring genes or disrupted intronic elements.
Presynaptic function is altered in hippocampal brain slices of HIP1-deficient mice demonstrating delayed recovery from synaptic depression and a reduction in paired-pulse facilitation.
The presence of a 110-kDa form of HIP1 in tumor cells was discovered. Upon sequencing of Hip1 DNA and message from these tumors, it was seen that this 110-kDa form of HIP1 is the product of splicing of a cryptic U12-type AT-AC intron.
Actin binding by Hip1 (huntingtin-interacting protein 1) and Hip1R (Hip1-related protein) is regulated by clathrin light chain
The product of this gene is a membrane-associated protein that colocalizes with huntingtin. This protein has similarities to cytoskeleton proteins and its interaction with huntingtin is thought to play a functional role in the cell filament network. Loss of normal huntingtin-HIP1 interaction in Huntington disease may contribute to a defect in membrane-cytoskeletal integrity in the brain. This gene could help in the understanding of the normal function of huntingtin and also the pathogenesis of Huntington disease. It also has been implicated in the pathogenesis of hematopoietic malignancies. Two transcript variants encoding different isoforms have been found for this gene.
huntingtin-interacting protein 1
, huntingtin-interacting protein I
, huntingtin interacting protein 1
, LOW QUALITY PROTEIN: huntingtin-interacting protein 1