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Findings indicate that Rph3A activity is linked to the aberrant synaptic localization of GluN2A-expressing NMDARs characterizing levodopa-induced dyskinesias; suggest that Rph3A/GluN2A complex could represent an innovative therapeutic target for those pathological conditions where NMDAR composition is significantly altered.
Rabphilin-3A is a major autoantigen in Lymphocytic infundibulo-neurohypophysitis (LINH). Autoantibodies to rabphilin-3A may serve as biomarker for the diagnosis of LINH and be useful for the differential diagnosis of Central diabetes insipidus.
rabphilin 3A loss correlated with dementia severity, cholinergic deafferentation, and increased beta-amyloid concentrations
Structural insights into the Ca2+ and PI(4,5)P2 binding modes of the C2 domains of rabphilin 3A and synaptotagmin 1.
Rabphilin-3A and Rab3A are present in normal mouse, rat, and human kidneys, with an exclusively glomerular expression and a comma-like pattern of positivity along the glomerular capillary wall, suggestive for podocyte staining.
Since rab3a participates in the docking and fusion of synaptic vesicles, and rabsa binding to alpha-synuclein is increased in Lewy body disease (LBD), it can be suggested that exocytosis of neurotransmitters may be impaired in LBD.
We found a reduction in rabphilin 3a, a protein involved in vesicle docking and recycling, in Huntington disease[HD] brains of grade III and IV. A deficient pre-synaptic transmitter release may underlie some symptoms of HD.
In mice, phosphorylation-regulated neutrophil polarization mechanism is driven by PKN1-mediated phosphorylation of a newly identified RAB21 effector RPH3A.
Rph3A interacts with GluN2A and PSD-95 forming a complex that regulates NMDARs stabilization at postsynaptic membranes.
a possible role in glomerulopathies
Our results indicate that a decrease in mRNA levels underlie the depletion of protein levels of rabphilin 3A, and we suggest that this reduction may be involved in causing impaired synaptic transmission in R6/1 mice.
rabphilin, by interacting with alpha-actinin, organizes the cell cytoskeleton to facilitate granule localization within F-actin-rich regions
Binding of rabphilin to SNAP-25 regulates exocytosis of synaptic vesicles after the readily releasable pool has either been physiologically exhausted by use-dependent depression, or has been artificially depleted by deletion of synaptobrevin.
Our results suggest that rabphilin, a protein present in presynaptic terminals, could play a role in the late phase of L-LTP.
Exocytosis of neurotransmitters and hormones is fundamental to synaptic neurotransmission and cell-cell communication. RAB3A (MIM 179390) is a small G protein that is thought to act at late stages of exocytosis, and RPH3A is a RAB3A effector (Lin et al., 2007
, rabphilin 3A homolog
, Doc2 family
, likely ortholog of mouse rabphilin 3A