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After HIP1 expression was blocked by siRNAs, EGFR (show EGFR Proteins) endocytosis was accelerated and this effect was dependent on the EGF (show EGF Proteins) concentration. This endocytosis was colocalized with clathrin expression. These findings indicate that the inhibition of HIP1 can accelerate the endocytosis and degradation of EGFR (show EGFR Proteins)
Data suggest that GLP1R (show GLP1R Proteins) signaling in pancreatic beta-cells leading to insulin (show INS Proteins) secretion involves interactions of GLP1R (show GLP1R Proteins) with HIP1, SNX1 (show SNX1 Proteins), and SNX27 (show SNX27 Proteins); HIP1 appears to regulate coupling of cell surface GLP1R (show GLP1R Proteins) activation with endocytosis; SNX1 (show SNX1 Proteins) and SNX27 (show SNX27 Proteins) appear to control balance between GLP1R (show GLP1R Proteins) 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 (show RAB1A Proteins) 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 (show ITK Proteins) 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 (show EGFR Proteins) 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 (show NFASC Proteins), and olfactomedin-like 2a) are novel components of podocyte major processes and their expression in glomerular crescents supports their role in crescent (show SFRP5 Proteins) formation.
Huntingtin-interacting protein 1 (Hip1) functions in Notch (show NOTCH1 Proteins)-mediated neurogenesis and provides a functional link between Notch (show NOTCH1 Proteins) signaling and proteins related to Huntington disease (show HTT Proteins).
we show that M. tuberculosis impairs dendritic cell cytokine secretion, maturation, and antigen presentation through the cell envelope-associated serine hydrolase (show SERHL Proteins), Hip1.
HIP1 association with and phosphorylation mediated by EGFR (show EGFR Proteins) and EGFRvIII.
Huntingtin-interacting protein 1 is a Merkel cell carcinoma marker that interacts with c-Kit
Results show that pro-apoptotic Hippi (show IFT57 Proteins)-Hip-1 heterodimers can recruit procaspase-8 into a complex of Hippi (show IFT57 Proteins), 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 (show GRIA3 Proteins) receptor trafficking
mice deficient in both HIP1 and HIP1r (show HIP1R Proteins) 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 (show GRIN1 Proteins) functions and that both HIP1 and htt (show HTT Proteins) participate in NMDA-induced cell death.
Degenerative phenotypes seen in knockout mice are due mainly to HIP1 and HIP1r (show HIP1R Proteins) protein deficiency rather than altered expression of neighboring genes or disrupted intronic elements.
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