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Human Polyclonal PCNT Primary Antibody for ICC, IF - ABIN253210
Basten, Willekers, Vermaat, Slaats, Voest, van Diest, Giles: Reduced cilia frequencies in human renal cell carcinomas versus neighboring parenchymal tissue. in Cilia 2013
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Human Polyclonal PCNT Primary Antibody for ICC, IF - ABIN4344848
Pasdeloup, Labetoulle, Rixon: Differing effects of herpes simplex virus 1 and pseudorabies virus infections on centrosomal function. in Journal of virology 2013
Show all 2 Pubmed References
The partial loss of these structures may largely explain the complex centriole, centrosome and cilium defects we observe in Plp mutant cells.
Cnn and PLP directly interact at two defined sites to coordinate the cell cycle-dependent rearrangement and scaffolding activity of the centrosome to permit normal centrosome organization, cell division, and embryonic viability.
Basal body formation in the male testes and the production of functional sperm does not rely on the PLP-CaM interaction, whereas production of functional mechanosensory neurons does.
Data indicate that interphase centrioles are closely associated with Sas-4, Spd-2, Polo kinase, Pericentrin-like protein (Dplp), Asterless (Asl), Plk4 kinase, Centrosomin (Cnn) and gamma-tubulin.
identification of CP309 which can bind to calmodulin; it is is required for microtubule nucleation mediated by centrosomes and it interacts with the gamma-tubulin small complex
We also find that Cep57 binds to the well-conserved PACT domain of pericentrin.
High pericentrin expression is associated with Disruptive Cilia Formation in down syndrome.
we identified two novel mutations in the PCNT gene associated with Microcephalic osteodysplastic primordial dwarfism type II and intracranial aneurysms
PCNT has to be phosphorylated by PLK1 to be a suitable substrate of separase.
Cep68 degradation allows Cep215 removal from peripheral pericentriolar material (PCM) preventing centriole separation following disengagement, PCNT cleavage mediates Cep215 removal from core of the PCM to inhibit centriole disengagement and duplication
The CEP215-pericentrin interaction is required for centrosome maturation and subsequent bipolar spindle formation during mitosis.
Data suggest that changes in the expression levels of PCNT in DS subjects may be involved into the molecular mechanism of Down's syndrome.
PCNT gene mutation is associated with hematological abnormalities in patients with microcephalic osteodysplastic primordial dwarfism type II.
Che-1 depletion abolishes the ability of Chk1 to bind pericentrin and to localize at centrosomes, which, in its turn, deregulates the activation of centrosomal cyclin B-Cdk1 and advances entry into mitosis.
The pericentrin B cleavage is essential for timely centriole disengagement and duplication.
Kendrin is a novel and crucial substrate for separase at the centrosome, protecting the engaged centrioles from premature disengagement and thereby blocking reduplication until the cell passes through mitosis.
Expression of RRP1B, PCNT, KIF21A and ADRB2 in leucocytes of Down's syndrome subjects, was analyzed.
The pericentrin (PCNT), a PCM protein, was specifically phosphorylated by PLK1 during mitosis.
PCNT has a crucial role in tooth development; teeth of a patient with a novel homozygous mutation p.Glu1154X are probably the smallest ever reported.
Severe insulin resistance and premature diabetes are common features of PCNT deficiency but are not congenital.
Microcephalic osteodysplastic primordial dwarfism type II is a genetically homogeneous condition due to loss-of-function of pericentrin.
Results found no significant association between the pericentrin gene and schizophrenia in the Japanese population. This gene may not play a major role independently in the etiology of SZ.
The NESs and NLS of pericentrin are essential for its subcellular localization and nucleocytoplasmic trafficking during the cell cycle.(Pericentrin)
Data suggest that pericentrin may regulate the intracellular distribution and secretion of insulin.
these results suggest that kendrin anchors Nek2A and suppresses its kinase activity at the centrosomes, and thus, is involved in the mechanism to prevent premature centrosome splitting during interphase.
experiments demonstrate a role for Pericentrin in modulating Piezo2 activity and membrane expression in somatosensory neurons
Meiotic division is highly error-prone in the absence of Pcnt and disrupted acentriolar microtubule-organizing centers.
Pericentrin is a key functional component of the unique acentriolar MTOCs of mouse oocytes, and plays an important role in regulating meiotic spindle assembly and/or stability.
The mouse Pcnt(-/-) phenotype was associated with misdirected ventricular septal growth in the heart, decreased proliferative symmetric divisions in brain neural progenitors, and increased misoriented divisions in fibroblasts.
Findings suggest distinct functional roles of several Pcnt variants in different ciliated tissues and sensory neurons, like the olfactory epithelium and the retina of the mouse
A mutation in the pericentrin gene causes abnormal interneuron migration to the olfactory bulb in mice
results confirm that MT1-MMP cleaves pericentrin-2 in humans but not in mice and that mouse models of cancer probably cannot be used to critically examine MT1-MMP functionality
Pcnt was shown to be localized to the base of primary cilia in multiple embryonic tissues, in agreement with a recent study demonstrating the involvement of Pcnt in primary cilia formation using cultured mammalian cells.
Pericentrin forms complexes with CHD3 and CHD4, but a distinct CHD3-pericentrin complex is required for centrosomal anchoring of pericentrin/gamma-tubulin and for centrosome integrity.
pPKCdelta(Thr505) interacts with MTOC-associated proteins pericentrin and gamma-tubulin, and plays a role in meiotic spindle organization in oocytes
pericentrin is essential for the assembly of chemosensory cilia of olfactory receptor neurons, but it is not globally required for cilia formation in mammals.
The protein encoded by this gene binds to calmodulin and is expressed in the centrosome. It is an integral component of the pericentriolar material (PCM). The protein contains a series of coiled-coil domains and a highly conserved PCM targeting motif called the PACT domain near its C-terminus. The protein interacts with the microtubule nucleation component gamma-tubulin and is likely important to normal functioning of the centrosomes, cytoskeleton, and cell-cycle progression. Mutations in this gene cause Seckel syndrome-4 and microcephalic osteodysplastic primordial dwarfism type II.
, drosophila pericentrin like protein
, lethal (3) s2172
, pericentrin-like protein
, pericentrin/AKAP450 centrosomal targeting
, pericentrin B
, DIP2 disco-interacting protein 2 homolog A
, pericentrin (kendrin)
, pericentrin 2 (kendrin)
, pericentrin 2