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mutation-induced stabilization of a partially folded state can enhance profilin-1 aggregation and thereby contribute to the pathogenicity of the mutations
Data suggest that profiling-1 (PFN1) preferentially binds to Huntingtin N-terminal fragment (HTT-NTF) M-phase species and destabilizes aggregation and phase separation by shifting concentration boundaries for phase separation to higher values through a process known as polyphasic linkage; this phenomena occurs irrespective of polyglutamine length in HTT-NTF.
profilin 1 expression may be involved in the pathophysiology of bronchopulmonary dysplasia via dysregulation of actin binding proteins
Variants of rs238243 and rs238238 might regulate profilin1 expression by epigenetic modification and indirectly affects the susceptible threshold of hypertension in Chinese Han population.
Results suggested that the RhoA/ROCK1 pathway activated by excessive ROS is responsible for profilin-1-mediated endothelial damage.
PFN1 could promote autophagy through taking part in Beclin1 complex and contribute to bortezomib resistance, which may become a novel molecular target in the therapy of MM.
Loss of PFN1 in tumor cells has been associated with lymph node invasion and metastasis in other tumor types, strengthening the argument that the protein has the potential to be a tumor suppressor in late-stage oral squamous cell carcinoma.
Guttiferone K effectively suppresses the motility and metastasis of hepatocellular carcinoma cells mainly by restoration of aberrantly reduced PFN1 protein expression
Results collectively suggest that PFN1 promotes cell migration and adhesion in bladder cancer models.
These results suggest that although mutant PFN1 aggregation may contribute to neurodegeneration, it does not trigger its onset. Importantly, these experiments establish a progressive disease model that can contribute toward identifying the mechanisms of ALS pathogenesis and the development of therapeutic treatments.
One potential mechanism for C71G-PFN1 to initiate Amyotrophic lateral sclerosis might be the abnormal interaction with membranes as recently established for SOD1 mutants.
Expression of PFN1 mutants induces accumulation of TDP-43, and promotes conversion of normal TDP-43 into an abnormal form. These results provide new insight into the mechanisms of TDP-43 proteinopathies and other diseases associated with amyloid-like protein deposition.
We suggest that reduction of PFN-1 expression by elevated levels of PrP(c) may contribute to protective effects PrP(c)-overexpressing SH-SY5Y cells confer against STS-induced apoptosis
this study shows that in pancreatic cancer patients, PFN1 expression is substantially decreased in peripheral CD8(+) T cells
mutant profilin1 in various diseases with an emphasis on its contribution to the pathogenesis of amyotrophic lateral sclerosis (Review)
Data suggest 2 major isoforms of profilin (Pfn1 and Pfn2) are co-regulated by a common mechanism involving the action of MKL1 [megakaryoblastic leukemia (translocation) 1 protein] that is independent of its SRF- (serum-response factor)-related activity; cellular externalization of Pfn1, rather than transcription, is affected by the perturbations of MKL1; MKL1 can influence cell migration by modulating Pfn1 expression.
novel profilin-1 variants associated with amyotrophic lateral sclerosis
We found that ARP3 and profilin1 were 2 binding partners of LMO2, primarily in cytoplasm. LMO2. LMO2 mediated the assembly of a complex including ARP3, profilin1, and actin monomer, increased actin monomer binding to profilin1, and promoted lamellipodia/filopodia formation in basal-type breast cancer cells.
These observations indicate that our novel profilin1 mutant mouse line may provide a new ALS model with the opportunity to gain unique perspectives into mechanisms of neurodegeneration that contribute to ALS pathogenesis.
These data suggest that Familial Amyotrophic Lateral Sclerosis-linked PFN1 mutations exacerbate TDP-43-induced neurodegeneration in a gain-of-function manner, possibly by shifting the localization of TDP-43 from nuclei to cytoplasm.
Profilin 1-mediated cytoskeletal rearrangements regulate integrin function in mouse platelets.
Profilin1 is expressed in osteocytes and regulates cell shape, migration and bone mass.
overexpression of profilin is sufficient to induce cardiomyocyte hypertrophy and sarcomeric remodelling, and silencing of profilin attenuates the hypertrophic response
Pfn1 is a novel target of BMP and suppresses BMP-induced differentiation of osteoblasts at least in part via transcriptional event.
knockdown of either profilin 1 or profilin 2a led to a significant decrease in cell spreading of astrocytes. Moreover, both isoforms proved to be crucial for forskolin-induced astrocytic stellation.
Inactivation of profilin 1 impaired the radial migration of cerebellar granule neurons
Megakaryocyte-specific Profilin1-deficiency alters microtubule stability and causes a Wiskott-Aldrich syndrome-like platelet defect.
Depleting FMNL1, another Formin family member, resulted in reduced mDia1 expression, while RhoA inhibition did not alter mDia1 expression, which indicated that there was a FMNL1-mDia1-Profilin1 signaling pathway in mouse oocytes.
association of cortactin with Pfn-1 is regulated by c-Abl-mediated cortactin phosphorylation
In glioblastomas endothelial cell-specific Pfn-1 phosphorylation elevates HIF-1alpha expression leading to vascular abnormalities and tumor progression.
Pfn1 as a key effector of the integrin linked kinase/Rho/ROCK pathway which acts in parallel with integrin beta1/LCK/Rac1 and regulates Schwann cells lamellipodia formation, radial sorting and myelination during peripheral nervous system maturation.
pfn1 at least partially acts through the axis of pfn1/Galpha13/EGR1 to regulate stem cell retention and metabolism in the bone marrow.
findings indicate that pfn haploinsufficiency protects against diet-induced insulin resistance and inflammation by modulating white adipose tissue immune homeostasis.
The results of this study found that the profilin1 is crucially important for brain development, but dispensable for the physiology of excitatory synapses.
Recognition of profilin by Toll-like receptor 12 is critical for host resistance to Toxoplasma gondii.
It was shown that activation of VEGF receptor kinase-2 and Src induces profilin 1 phosphorylation in the cell leading edge, promoting profilin 1 binding to actin and actin polymerization. Profilin 1 phosphorylation is critical for angiogenesis.
Pfn1 is a critical molecule for the skeletal development, and this could be at least in part associated with the retardation of cell migration
ACE2 deficiency enhances angiotensin II-mediated aortic profilin-1 expression, inflammation and peroxynitrite production.
Loss of profilin1 had no adverse effects on the morphology and function of excitatory synapses.
Profilin1 ablation from mouse brains leads to a cerebellar hypoplasia, aberrant organization of cerebellar cortex layers and ectopic Cerebellar granule neurons (CGNs).
biophysical analysis reveals that the open nucleotide pocket of the profilin/actin x-ray structure is unstable and closes in the absence of profilin
nitric oxide and free radicals produced under different conditions could alter the functions of profilin through nitration, such as its interaction with actin and poly (l-proline).
Profilin regulates actin dynamics both within the cytoplasm and inside the nuclei of developing mammalian embryos.
Phosphorylation studies indicate that profilin dimers are not phosphorylated while teramers are preferentially phosphorylated over monomers.
PRF1 coordinates the stochastic dynamic properties of actin filaments by modulating formin-mediated actin nucleation and assembly during plant cell expansion.
formed a filamentous network likely associated with actin filaments
protein CYK-1 and the profilin PFN-1 mediate the Arp2/3-independent assembly of cortical microfilaments and are required for cytokinesis in the early embryo
Thus the model organism Caenorhabditis elegans expresses three profilin isoforms and is the first invertebrate animal with tissue-specific profilin expression.
profilin promotes actin organisation
This gene encodes a member of the profilin family of small actin-binding proteins. The encoded protein plays an important role in actin dynamics by regulating actin polymerization in response to extracellular signals. Deletion of this gene is associated with Miller-Dieker syndrome, and the encoded protein may also play a role in Huntington disease. Multiple pseudogenes of this gene are located on chromosome 1.
, profilin 1
, epididymis tissue protein Li 184a
, profilin I
, actin binding protein