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Both FMRP (show FMR1 Proteins) deficiency in Fmr1 (show FMR1 Proteins)(I304N) mice and Fmr1 (show FMR1 Proteins) knockdown impeded the axonal delivery of miR (show MLXIP Proteins)-181d, Map1b (show MAP1B Proteins), and Calm1 and reduced the protein levels of MAP1B (show MAP1B Proteins) and calmodulin in axons.
The association of calcium-bound calmodulin (CaM) with DREAM is mediated by a short amphipathic amino acid sequence located between residues 29 and 44 on DREAM.
Calcium plays a role in regulating the expression and function of beta-adducin to sustain normal organization of the spectrin-based cytoskeleton and the differentiation properties in keratinocytes through the calmodulin/EGFR/cadherin signaling pathway.
Data suggest that Cys3602 in RyR2 (ryanodine receptor 2) plays important role in activation/termination of Ca2+ release, but it is not essential for calmodulin regulation of RyR2.
CaM plays an active role in shaping both the spatial and temporal aspects of calcineurin-mediated calcium signaling.
Calm1 signaling pathway is essential for the migration of mouse precerebellar neurons.
Ca(2+) binding to calmodulin induces major conformational changes in both IQ motifs and the post-IQ domain and increases flexibility of the myosin-1c tail.
Using mass spectrometry this study identified calmodulin as a calcium-dependent GluN2A (show GRIN2A Proteins) binding partner.
new insights into the role of BTK (show BTK Proteins), an important target for autoimmune diseases, in B cell activation (show BLNK Proteins)
The relationships between the interaction of alphaCaMKII with CaM and the conformational change of alphaCaMKII, were investigated.
The unique C terminus of the calcineurin isoform CNAbeta1 confers non-canonical regulation of enzyme activity by Ca(2 (show CA2 Proteins)+) and calmodulin
The main functional derangement in CALM1-F142L was prolonged repolarization with altered rate-dependency and sensitivity to beta-adrenergic stimulation.
These results reveal that mTOR (show FRAP1 Proteins) is a new type of calmodulin-dependent kinase, and TRPML1 (show MCOLN1 Proteins), lysosomal calcium and calmodulin play essential regulatory roles in the mTORC1 signaling pathway.
The structural basis for the recognition of EEF2K (show EEF2K Proteins) by calmodulin has been presented.
irradiated tumor cells were observed to significantly up-regulate the expression of calcium-binding proteins CALM1, CALU (show CALU Proteins), and RCN1 (show RCAN1 Proteins), suggesting important roles for these mediators in promoting irradiated tumor cell survival during hypoxia
Calcium modulates calmodulin-ACTN1 (show ACTN1 Proteins) interaction with and agonist-dependent internalization of the adenosine A2A receptor (show ADORA2A Proteins).
Data suggest that GRB10 (show GRB10 Proteins) and GRB14 (show GRB14 Proteins) are both Ca2 (show CA2 Proteins)+-dependent CaM-binding proteins; more than one CaM-binding site and/or accessory CaM-binding sites appear to exist in GRB10 (show GRB10 Proteins) and GRB14 (show GRB14 Proteins), as compared to a single one present in GRB7 (show GRB7 Proteins). (GRB10 (show GRB10 Proteins) = growth factor receptor-bound protein 10 (show GRB10 Proteins); GRB14 (show GRB14 Proteins) = growth factor receptor-bound protein 14 (show GRB14 Proteins); CaM = calmodulin; GRB7 (show GRB7 Proteins) = growth factor receptor-bound protein 7 (show GRB7 Proteins))
studies demonstrate that UBE3B (show UBE3B Proteins) is an E3 ubiquitin ligase (show MUL1 Proteins) and reveal that the enzyme is regulated by calmodulin. Furthermore, the modulation of UBE3B (show UBE3B Proteins) via calmodulin and calcium implicates a role for calcium signaling in mitochondrial protein (show COX6B2 Proteins) ubiquitylation, protein turnover, and disease
Up-regulation of miR (show MLXIP Proteins)-335 suppressed CaM protein expression in patients with acute ischemic stroke, and CaM was confirmed as a direct target of miR (show MLXIP Proteins)-335.
The unique properties of the CaM-F142L mutation may provide novel clues on how to suppress excessive RyR2 Ca(2+) release by manipulating the CaM-RyR2 interaction.
This gene encodes a member of the EF-hand calcium-binding protein family. It is one of three genes which encode an identical calcium binding protein which is one of the four subunits of phosphorylase kinase. Two pseudogenes have been identified on chromosome 7 and X. Multiple transcript variants encoding different isoforms have been found for this gene.
, Calmodulin 1 (phosphorylase kinase, delta)
, phosphorylase kinase, delta subunit
, prepro-calmodulin 1