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These findings suggest that lysoPC induces CaM phosphorylation at Tyr (show TYR Antibodies)(99) by a Src (show SRC Antibodies) family kinase and that phosphorylated CaM activates PI3K to produce PIP3, which promotes TRPC6 (show TRPC6 Antibodies) translocation to the cell membrane.
calmodulin promotes catalysis by shaping the physical and temporal conformational behaviors of NOS (show NOS Antibodies).
examination of Ca(+2 (show CA2 Antibodies))-calmodulin showing highly significant correlations between surface area and side-chain contact predictions for individual side chains and the crystal structure, is reported.
Fluorescence decays of fluorescently labeled CaM bound to eNOS (show NOS3 Antibodies) reveal four distinct conformational states and single-molecule fluorescence trajectories show multiple fluorescence states with transitions between states
key regulatory role of CaM involves the stabilization of structural intermediates and precise positioning of the pivot for the FMN (show FMN1 Antibodies) domain tethered shuttling motion to accommodate efficient and rapid electron transfer in the homodimer of eNOS (show NOS3 Antibodies).
The results provide a basic idea that could lead to the development of small peptides binding with high affinity to CaM and inhibiting Ca(2 (show CA2 Antibodies))-CaM complex formation in the future.
CaM is collapsed around the adenylyl cyclase 8 (show ADCY8 Antibodies) peptides that binds to CaM in an antiparallel orientation.
Calmodulin bound to the first IQ motif is responsible for calcium-dependent regulation of myosin 5a (show MYO5A Antibodies).
Data indicate that the information obtained can enhance understanding of how CaM interacts with K-RasB in physiological environments.
we propose a model in which the partial unfolding of the suppressor domain by apo (show C9orf3 Antibodies)-CaM and the stepwise binding of the N lobe (show LTF Antibodies) of CaM to the suppressor domain are important elements of calcium/CaM inhibition of IP(3)R (show ITPR1 Antibodies)
A novel KRIT1 heterozygous nonsense mutation (c.1864C>T) segregated with familial cerebral cavernous malformation in a Chinese family.
A novel heterozygous insertion KRIT1 mutation identified in cerebral cavernous malformation patient. mRNA level of KRIT1 were significantly decreased in FCCM subjects.
A novel nonsense mutation in CCM1 were detected in cerebral cavernous malformations patient.
nuclear-cytoplasmic shuttling of ICAP1 (show ITGB1BP1 Antibodies) influences both integrin activation and KRIT1 localization, presumably impacting nuclear functions of KRIT1.
New Krit1 mutations segregated with cerebral cavernous malformation in Chinese families.
Studies suggest that the 3 proteins of the Cerebral Cavernous Malformations (CCM) complex KRIT1/CCM1, CCM2/malcavernin (show CCM2 Antibodies) and CCM3/PDCD10 (show PDCD10 Antibodies) not only require one another for reciprocal stabilization, but also act as a platform for signal transduction.
Valproic acid reduces intracellular ROS (show ROS1 Antibodies) level by the modulation of KRIT1 and its correlated proteins, FoxO1 (show FOXO1 Antibodies), SOD2 (show SOD2 Antibodies), and cyclin D1 (show CCND1 Antibodies) in mesenchymal stromal cells.
KRIT1 protects endothelial integrity during mechanical stress and trap6 exposure.
Novel CCM1 deletion mutation segregated with cerebral cavernous angioma in a Chinese family.
Case Report: cerebral cavernous malformations and unilateral moyamoya disease in a patient with a new mutation in the KRIT-1 /CCM1 gene.
Lesions develop in a stereotypic location and pattern, preceded by endothelial hypersprouting as confirmed in a zebrafish model of disease. The vascular defects seen with loss of Ccm1 suggest a defect in endothelial flow response.
CCM1 silencing in endothelial cells caused decreased Notch3 (show NOTCH3 Antibodies) activity in cocultured pericytes
Data indicate that vascular endothelial growth factor (VEGF) signaling contributes to modifying endothelial function in Krev-interaction trapped 1 (KRIT1)-deficient cells and microvessel permeability in Krit1(+/-) mice.
The CCM1 loss resulted in ICAP-1 (show ITGB1BP1 Antibodies) destabilization, which increased beta1 integrin activation and led to increased RhoA (show RHOA Antibodies)-dependent contractility.
Data indicate an integral role for KRIT1 in microvessel homeostasis and the vascular response to inflammation.
Pdcd10 (show PDCD10 Antibodies) has a different role in cerebral cavernous malformation than Ccm2 (show CCM2 Antibodies) and Krit1
Results suggests that KRIT1 limits the accumulation of intracellular oxidants and prevents oxidative stress-mediated cellular dysfunction and DNA damage by enhancing the cell capacity to scavenge intracellular ROS (show ROS1 Antibodies).
The KRIT1-CCM2 (show CCM2 Antibodies) interaction regulates endothelial junctional stability and vascular barrier function by suppressing activation of the RhoA (show RHOA Antibodies)/ROCK signaling pathway.
KRIT1 regulates beta-catenin (show CTNNB1 Antibodies) signaling, and Krit1(+/-) mice are more susceptible to beta-catenin (show CTNNB1 Antibodies)-driven intestinal adenomas.
evidence of differential Krit1 and Rap1A (show RAP1A Antibodies) expression during mouse ontogenesis and suggest a more widespread functional significance of Krit1, not restricted to vascular endothelial cells.
CCM3 (show PDCD10 Antibodies) signals through sterile 20-like kinases to regulate both endothelial and epithelial cell junctions in development and disease.
endothelial cellular morphogenesis is regulated by CCM1 proteins during development and pathogenesis. [CCM1]
the direct interaction between Rap1 (show TERF2IP Antibodies) and KRIT1 is required for KRIT1 function in cardiovascular development.
Ccm1 has been identified as a key angiogenic modulator in microvascular tubulogenesis.
Zebrafish embryos with the recessive lethal mutations santa (san) and valentine (vtn (show VTN Antibodies)) do not thicken, but do add the proper number of cells to the myocardium.
This gene encodes a protein containing four ankyrin repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and multiple NPXY sequences. The encoded protein is localized in the nucleus and cytoplasm. It binds to integrin cytoplasmic domain-associated protein-1 alpha (ICAP1alpha), and plays a critical role in beta1-integrin-mediated cell proliferation. It associates with junction proteins and RAS-related protein 1A (Rap1A), which requires the encoded protein for maintaining the integrity of endothelial junctions. It is also a microtubule-associated protein and may play a role in microtubule targeting. Mutations in this gene result in cerebral cavernous malformations. Multiple alternatively spliced transcript variants have been found for this gene.
krev interaction trapped protein 1
, Krev interaction trapped protein 1
, calmodulin 2 (phosphorylase kinase, delta)
, ankyrin repeat-containing protein Krit1
, cerebral cavernous malformations 1 protein
, krev interaction trapped 1
, cerebral cavernous malformations 1 protein homolog