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The protein encoded by PICK1 contains a PDZ domain, through which it interacts with protein kinase C, alpha (PRKCA). Additionally we are shipping and many more products for this protein.
Showing 3 out of 3 products:
a dual role of PICK1 in regulating macrophage polarization
This study demonstrated that d-serine provent the behavioral deficits in adult Pick1 knockout mice.
PICK1 is an important regulator of P2Y6R (show P2RY6 Proteins) expression and microglial phagocytosis.
knocking-out PICK1 gene casts the neuroprotection effect by reducing ASICs current and the calcium transients in OGD (show FGFR1 Proteins)-Rep neuronal cells
ICA1L forms BAR-domain complexes with PICK1 and is crucial for acrosome formation in spermiogenesis.
results indicate that PICK1 is a crucial regulator in glutathione homeostasis and may play important roles in oxidative stress.
In cultured neurons, PICK1 deletion increases surface AMPARs and blocks Abeta42-induced reduction in surface GluA2 (show GRIA2 Proteins).
This study demonstrated that PICK1 functions in vesicle biogenesis and is necessary to maintain normal vesicle numbers and size.
C-terminal domain of ICA69 (show ICA1 Proteins) interacts with PICK1 and acts on trafficking of PICK1-PKCalpha (show PKCa Proteins) complex and cerebellar plasticity.
we found that PICK1's expression in testis rescued the spermatogenic abnormalities and male infertility in Pick1 knockout mice. Our results indicate that the infertility is caused by the lack of PICK1 in the testis rather than in other organs.
We propose that PICK1 negatively regulates neoplastic infiltration of astrocytic tumors and that manipulation of PICK1 is an attractive possibility for therapeutic intervention
PICK1 domain ACT links PICK1-associated vesicles to a motility factor, likely myosin, but, contrary to previous reports, PICK1 neither binds nor inhibits Arp2 (show ACTR2 Proteins)/3 complex.
Unlike accessory domains in other BAR domain proteins, the positioning of the PDZ domains is flexible, enabling PICK1 to perform long-range, dynamic scaffolding of membrane-associated proteins.
Data indicate three principal binding modes can account for protein interacting with C-kinase 1 (PICK1) PDZ domains binding specificity.
PICK1 promotes Ago2 (show EIF2C2 Proteins) localization at endosomal compartments in neuronal dendrites and inhibits Ago2 (show EIF2C2 Proteins) function in translational repression following neuronal stimulation.
These data indicate that Pick1 is involved in regulating the cell-cell junction in epithelial cells.
Family-based association study failed to observe a statistically significant association for any of the genotyped SNPs in the PICK1 gene and attention-deficit hyperactivity disorder.
PICK1 increases caveolin-mediated endocytosis, ubiquitination and degradation of TGF-beta type I receptor (show TGFBR1 Proteins).
The binding affinities of all major PICK1 interacting proteins are reported and the effects of PICK1 mutations on these interactions are described.
The protein encoded by this gene contains a PDZ domain, through which it interacts with protein kinase C, alpha (PRKCA). This protein may function as an adaptor that binds to and organizes the subcellular localization of a variety of membrane proteins. It has been shown to interact with multiple glutamate receptor subtypes, monoamine plasma membrane transporters, as well as non-voltage gated sodium channels, and may target PRKCA to these membrane proteins and thus regulate their distribution and function. This protein has also been found to act as an anchoring protein that specifically targets PRKCA to mitochondria in a ligand-specific manner. Three transcript variants encoding the same protein have been found for this gene.
protein interacting with PRKCA 1
, PRKCA-binding protein
, protein kinase C, alpha binding protein
, protein kinase C-alpha-binding protein
, protein that interacts with C kinase 1
, protein interacting with C kinase 1