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vps35 belongs to a group of vacuolar protein sorting (VPS) genes. Additionally we are shipping vps35 Proteins (3) and many more products for this protein.
Showing 10 out of 45 products:
Chinese Hamster Polyclonal vps35 Primary Antibody for ICC, IF - ABIN250175
Hong, Yang, Zhang, Niu, Li, Zhao, Liu: The retromer component SNX6 interacts with dynactin p150(Glued) and mediates endosome-to-TGN transport. in Cell research 2009
Show all 14 Pubmed References
Human Monoclonal vps35 Primary Antibody for ELISA, WB - ABIN565910
Prosser, Tran, Schooley, Wendland, Ngsee: A novel, retromer-independent role for sorting nexins 1 and 2 in RhoG-dependent membrane remodeling. in Traffic (Copenhagen, Denmark) 2010
Show all 3 Pubmed References
Human Polyclonal vps35 Primary Antibody for IHC, IHC (p) - ABIN4365839
Yin, Liu, He, Zhou, Yuan, Zhao: Vps35-dependent recycling of Trem2 regulates microglial function. in Traffic (Copenhagen, Denmark) 2016
Human Polyclonal vps35 Primary Antibody for IHC, ELISA - ABIN185182
Zhang, Yu, Gao, Fu, Dai, Zhao, Zheng, Zhao: Cloning and characterization of human VPS35 and mouse Vps35 and mapping of VPS35 to human chromosome 16q13-q21. in Genomics 2001
Show all 2 Pubmed References
The in vivo effects of P316S, D620N and L774M of VPS35 using Drosophila as a model, were investigated.
The findings of this study indicate that the VPS35 may play a crucial role in alpha-synucle in degradation by modulating the maturation of cathepsin D (show CTSD Antibodies) and might thereby contribute to the pathogenesis of the disease.
overexpression of Vps35 ameliorates the pathogenic mutant LRRK2 (show LRRK2 Antibodies) eye phenotype in a Drosophila model of Parkinson's disease
Vps35 negatively regulates actin (show ACTB Antibodies) polymerisation, and genetic interactions suggest that some of the endocytic and signalling defects of vps35 mutants are due to this function
Results provide evidence for a critical role of Vps35 in mouse corneal dystrophy; suggest that SLC4A11 (show SLC4A11 Antibodies) appears to be a Vps35/retromer cargo, and Vps35-regulation of SLC4A11 (show SLC4A11 Antibodies) trafficking may underlie Vps35/retromer regulation of corneal dystrophy.
Our study suggests that Vps35/retromer is responsible for recycling of Trem2 (show TREM2 Antibodies) in the regulation of microglial function such as proinflammatory responses.
Using in vivo knockdown of the critical retromer component VPS35, we demonstrate a specific role for this endosomal sorting complex in the trafficking of AMPA (show GRIA3 Antibodies) receptors during NMDA-receptor-dependent LTP (show SCP2 Antibodies) at mature hippocampal synapses.
the data presented in this manuscript demonstrate a critical function of VPS35 in regulating PTH1R (show PTH1R Antibodies) trafficking. This event and VPS35-interaction with PPP1R14C (show PPP1R14C Antibodies) appear to be essential for turning off PTH1R's endosomal signaling, and promoting PTH1R (show PTH1R Antibodies)-mediated catabolic response and bone remodeling.
These results provide evidence for VPS35's function in promoting spine maturation, which is likely through increasing AMPA (show GRIA3 Antibodies) receptor targeting to the postsynaptic membrane.
Deletion of the VPS35 gene in dopamine (DA) neurons resulted in Parkinson disease-like deficits, including loss of DA neurons and accumulation of alpha-synuclein.
These results suggest that VPS35 deficiency or mutation promotes Parkinson Disease (PD) pathogenesis, and reveals a crucial pathway, VPS35-Lamp2a-alpha-synuclein, to prevent PD pathogenesis.
Our studies reveal unexpected genetic and functional interactions between VPS35 and EIF4G1, two seemingly unrelated PD genes, and functionally connect them to alpha-synuclein pathobiology in yeast, worms, and mouse.
Vps35 is necessary for mouse retinal ganglion cell survival and regeneration.
VPS35 critically deregulates RANK signaling, thus restraining increased formation of hyperresorptive OCs and preventing osteoporotic deficits.
Present data support a role for perturbed VPS35 and retromer function in the pathogenesis of Parkinson's disease.
These findings provide new mechanistic insights into the role of VPS35 in the regulation of AIMP2 (show AIMP2 Antibodies) levels and cell death.
The retromer complex is a highly conserved membrane trafficking assembly composed of three proteins - Vps26 (show VPS26A Antibodies), Vps29 (show VPS29 Antibodies) and Vps35, which are impaired in neurodegenerative diseases. (Review)
It could interact with DRD1 (show DRD1 Antibodies) and regulate DRD1 (show DRD1 Antibodies) cell surface recycling, as well as DRD1 (show DRD1 Antibodies)- mediated dopamine signaling.
The absence of mutations in VPS35 genes reveals that they are uncommon causes of Parkinson disease in Brazil
VPS35 has been associated with autosomal dominant forms of Parkinson's disease with a high but incomplete penetrance .
results lend further support to the notion that VPS35-DLP1 (show DNM1L Antibodies) interaction is key to the retromer-dependent recycling of mitochondrial DLP1 (show DNM1L Antibodies) complex during mitochondrial fission and provide a novel therapeutic target to control excessive fission and associated mitochondrial deficits.
Silencing VPS35 increased N-Ras's association with cytoplasmic vesicles, diminished GTP (show AK3 Antibodies) loading of Ras, and inhibited mitogen-activated protein kinase (show MAPK1 Antibodies) signaling and growth of N-Ras (show NRAS Antibodies)-dependent melanoma cells.
deletion of VPS35 in yeast (vps35Delta) leads to a dose-dependent growth defect towards copper. This increased sensitivity could be rescued by transformation with yeast wild-type VPS35 but not by the expression of a construct harboring the yeast equivalent (i.e. D686N) of the most commonly identified VPS35-associated Parkinson disease mutation, p.D620N
the Vps35 R524W-containing retromer has a decreased endosomal association, which can be partially rescued by R55, a small molecule previously shown to stabilize the retromer complex, supporting the potential for future targeting of the retromer complex in the treatment of Parkinson disease.
This gene belongs to a group of vacuolar protein sorting (VPS) genes. The encoded protein is a component of a large multimeric complex, termed the retromer complex, involved in retrograde transport of proteins from endosomes to the trans-Golgi network. The close structural similarity between the yeast and human proteins that make up this complex suggests a similarity in function. Expression studies in yeast and mammalian cells indicate that this protein interacts directly with VPS35, which serves as the core of the retromer complex.
vacuolar protein sorting-associated protein 35
, vacuolar protein sorting 35 homolog (S. cerevisiae)
, vacuolar protein sorting 35 homolog
, vacuolar protein sorting 35-like
, vacuolar protein sorting 35
, Vacuolar protein sorting 35
, maternal embryonic message 3
, maternal-embryonic 3
, vesicle protein sorting 35