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Human PFN1 Protein expressed in Escherichia coli (E. coli) - ABIN666790
Harbeck, Hüttelmaier, Schluter, Jockusch, Illenberger: Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin. in The Journal of biological chemistry 2000
Show all 2 references for ABIN666790
Gain-of-toxic-function PFN1 gene mutation leads to conformational change of TDP-43 (show TARDBP Proteins) and to neurodegeneration in amyotrophic lateral sclerosis.
Profilin synergizes with chemotherapeutic drugs to induce tumor cell death by regulating NF-kappaB (show NFKB1 Proteins) and p53 (show TP53 Proteins). Thus, modulation of Profilin may be a useful strategy for effective combination therapy.
Mutations of profilin-1, associated with familial amyotrophic lateral sclerosis, increase the tendency of profilin-1 to aggregate and that such aggregation behavior is largely determined by the mutation-induced structural changes occurring in the folded state of the protein.
evidence, which suggests that Profilin increases tumour suppressor activity by regulating NF-kappaB (show NFKB1 Proteins).
Profilin-1 folding process occurs in the absence of thermodynamically stable partially folded states.
Actin independent mechanisms contribute to the pathogenicity of PFN1 T109M and possibly other PFN1 mutations.
expression of the ALS (show IGFALS Proteins)-associated actin-binding deficient mutant of PFN1 (PFN1(C71G)) results in increased dendritic arborisation and spine formation, and cytoplasmic inclusions in cultured mouse hippocampal neurons
PFN1 is a rare cause of ALS.
findings suggest that a destabilized form of PFN1 underlies PFN1-mediated ALS pathogenesis
Suggest that PFN1 plays a critical role in gastric carcinoma progression, and these effects are likely mediated through the integrin beta1/FAK (show PTK2 Proteins) pathway.
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 (show WASL Proteins) platelet defect.
Depleting FMNL1 (show FMNL1 Proteins), another Formin (show FMN1 Proteins) family member, resulted in reduced mDia1 expression, while RhoA (show RHOA Proteins) inhibition did not alter mDia1 expression, which indicated that there was a FMNL1 (show FMNL1 Proteins)-mDia1-Profilin1 signaling pathway in mouse oocytes.
association of cortactin (show CTTN Proteins) with Pfn-1 is regulated by c-Abl (show ABL1 Proteins)-mediated cortactin (show CTTN Proteins) phosphorylation
In glioblastomas endothelial cell-specific Pfn-1 phosphorylation elevates HIF-1alpha (show HIF1A Proteins) 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 (show GNA13 Proteins)/EGR1 (show EGR1 Proteins) to regulate stem cell retention and metabolism in the bone marrow.
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