In August of , they won the grand prize and audience favorite awards at the Gallo Center for the Arts talent show The Valley Talent Project , in which one of the judges was Robert Ulrich casting director of the Glee Project and Quantico. The Rykert Trio sincerely hopes and prays that their story and their music will encourage all to trust God with what ever challenges they may be facing. You can find their first two projects on all musical platforms for downloads and streaming. This album feature's the title song, "Healed" written by their dear friend, Joey Coray.
Stay tuned, as this project is due to be released this summer! Joe, who is classically trained has sung numerous tenor opera: Townsend Opera and musical theatre: Modesto Performing Arts leads for over 30 years. She has been involved with music her entire life. Noel has a natural God-given talent and has sung in several musicals, starting at the age of 6 and has also performed as a soloist for several years.
Besides singing, Noel is a hair stylist, wife to Michael LaRosa and mother to three beautiful children who also occasionally sing with the Trio.
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These biochemical assays are supported by microinjection studies in cultured fibroblasts, in which injection of GEF1 or the constitutively active mutant Rac1 V12 leads to increased cell spreading and lamellipodia formation, while injection of GEF2 or RhoA V14 causes an increase in stress fibre formation Ridley and Hall, ; Ridley et al. Potential interactions in Trio signal transduction.
The figure represents a generic Trio family member and incorporates biochemical and genetic data from different organisms. A region of the spectrin repeats of kalirin interacts with PAM and may regulate receptor internalization. Genetic interactions from Drosophila suggest that Trio functions with components of the Abl pathway including Fax and Ena , but the biochemical nature of this interaction is unclear.
Called kalirin, the full-length molecule has a domain structure nearly identical to that of Trio Fig. The different kalirin isoforms have distinct subcellular localizations; for example, the full-length kalirin is restricted to the soma of primary cortical neurons, whereas an isoform lacking the second GEF and kinase domains kalirin-7, also known as Duo is observed in a punctate pattern in neuronal processes Johnson et al.
This suggests potential functional differences between isoforms that require localization to specified cellular compartments.
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Although potential functions for kalirin have been suggested, including PAM internalization from the cell membrane Alam et al. Whereas Trio is expressed at moderate levels in all tissues, kalirin expression is specific to the central nervous system in the adult rat Debant et al. Although they possess slight structural differences, it is plausible that kalirin and Trio function in a similar manner in their different tissues.
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The observations that the N-terminal GEF domain of kalirin is capable of activating Rac1 in vitro and that expression of the domain in cultured fibroblasts results in cell spreading and lamellipodia formation are consistent with this idea Alam et al. Furthermore, it is unclear whether the kinase domains are active or display substrate specificity, although a highly related kinase named Duet is autophosphorylated in vitro Kawai et al.
Further biochemical studies should identify other signaling partners, shedding light on potential functions of Trio family members.
The above biochemical studies of Trio and kalirin have initiated our understanding of Trio signaling mechanisms in a cellular context, and data from model genetic systems have begun to shed light on potential roles of Trio signaling during development. It is not known whether this defect is directly tied to GTPase activation, but studies of Drosophila have shown a role for Rac activation in myoblast fusion Luo et al.
Thus, Trio appears to mediate fine-scale mapping of neuronal cell positions once the global arrangement of the brain has been established. Further analysis will determine whether other aspects of neuronal development, such as axon guidance, are also affected in mutant mice. The C. The fibronectin III domain could potentially interact with other cellular factors to facilitate or influence UNC function, but it remains to be determined what these factors may be and how this might differ from the function of Trio molecules in other species.
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Antibody staining and GFP fusions show that UNC is expressed generally in the developing embryo, with highest levels being observed in the nervous system Steven et al. The upstream signals that utilize UNC signaling in these diverse contexts are as yet unreported; however, Rac activation appears to be critical for UNC function, given that a point mutation abolishing exchange activity of the N-terminal GEF domain produces a strong loss-of-function mutant Steven et al.
The role of Rho activation is less clear; although a minigene lacking the sequence that encodes the C-terminal GEF domain rescues several unc mutants, it appears that these alleles still express C-terminal portions of the gene from alternative start sites and thus retain Rho exchange activity Steven et al. Steven and T. Pawson, personal communication.
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Adding a new chapter to the story, several research groups have recently described a Drosophila Trio homolog. As in the worm, Drosophila trio is expressed throughout the developing embryo, and high levels are observed in nervous tissues Awasaki et al. Mutations in trio produce pleiotropic axonal phenotypes in both the embryonic nervous system and retinal axon projections, including stalling, missed targets and inappropriate fasciculation Awasaki et al. These defects are similar to those observed in unc mutants, which suggests some conservation of cellular functions across evolutionary lines.
Consistent with this, in vivo rescue experiments show that GEF1, but not GEF2, activity is required for correct pathfinding of retinal axons Newsome et al.
Furthermore, a partial loss of trio function suppresses a gain-of-function retinal morphology phenotype of Drac1 but not DrhoA Bateman et al. Thus, the Rac-specific GEF1 appears to be the major signaling domain for retinal developmental processes that require Drosophila Trio, highlighting the importance of a signaling pathway involving Rac. The retinal axon defects observed in Drosophila trio mutants are similar to those of the previously identified mutant Pak-kinase Pak , which encodes the Drosophila homolog of the pactivated kinase PAK Hing et al.
In both trio and Pak mutants, retinal axons fail to recognize their appropriate synaptic targets, instead improperly fasciculating and extending into deeper regions of the brain. Dosage-sensitive genetic interactions between trio and Pak suggest that they may operate in a common pathway to regulate retinal axon guidance Newsome et al. Indeed, previous studies of the vertebrate homolog PAK have shown that it is a downstream effector of Rho family GTPases; activation of PAK kinase activity requires prior binding of its pbinding domain by GTP-bound Rac or Cdc42, which unleashes the kinase domain from a sterically hindered conformation Daniels and Bokoch, ; Hoffman and Cerione, Activated PAK then phosphorylates substrates that affect the actin cytoskeleton.
For example, PAK phosphorylation of myosin light chain kinase MLCK decreases phosphorylation of the regulatory subunit of myosin, altering actin-myosin contractility Sanders et al. Such changes in cytoskeletal dynamics might then aid in guiding a growth cone towards its appropriate target region Lin et al. Although genetic evidence in the Drosophila retina is consistent with a Pak pathway for Trio signaling, it is also possible that Pak activation occurs independently of Trio through activation of Rac by other GEFs such as PIX Manser et al. Future experiments should address the GEF specificity of Pak activation in different developmental events.
In response to extracellular cues, Nck binds to activated receptors at the cell surface through its SH2 domain, while simulaneously binding PAK through one of its three SH3 domains reviewed in McCarty, The subsequent recruitment to the membrane is important for PAK activation; artificial targeting of PAK to the membrane by myristilation can lead to activation of its kinase activity Lu et al. This relationship holds true in Drosophila , in which the Nck homolog Dreadlocks dock is required for proper development of retinal axons Garrity et al. As is the case for Pak and trio , mutations in dock cause axons to improperly fasciculate and extend past their appropriate targets.
Again, the primary function of Dock is presumably to bring Pak to the membrane, because axonal defects observed in dock mutants can be rescued by myristilated PAK Hing et al. Although the interaction between Pak and Dock is conserved in the Drosophila retina, the upstream receptors and signals that localize and activate Trio and Dock, and thus ultimately guide neurons, are as yet unknown.
It will be interesting to determine whether Trio also functions in this particular guidance system. Similarly, mutants of the LAR family phosphatase Dptp69D have an axonal phenotype resembling that of trio and dock in loss-of-function mutant retinas, which suggests that the phosphatase participates in similar signaling events Garrity et al. The physical interaction of LAR and Trio in humans provides an attractive model for RPTP signaling, but it is not clear whether this relationship exists in Drosophila , because the C-terminal portions of Trio that are responsible for phosphatase binding are not conserved in the fly Debant et al.
Abl, see below , rather than through a direct physical interaction. Although PAK is a strong candidate for transduction of Trio signals, several lines of evidence suggest that Trio must also operate through alternative pathways. For example, retinal axon phenotypes in trio and Pak mutants are similar but not identical. In trio mutants, a subset of axons stop short of their target regions rather than projecting past them; this defect is not observed in retinas lacking Pak or dock Garrity et al.https://tingderthemacwhe.ga
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Thus, PAK must convey only targeting information, whereas other molecules must be responsible for axonal extension directed by Trio. This is consistent with embryonic analyses, in which mutations in trio cause an extension defect in the motor nerve ISNb Awasaki et al. Pak -mutant embryos have yet to be described, but mutations in dock cause a much milder ISNb phenotype and therefore cannot entirely account for Trio signaling Desai et al. However, mutations in the tyrosine kinase Abl cause an ISNb defect that is indistinguishable from that of trio mutants Wills et al.
Furthermore, altering the genetic dose of trio or Abl enhances CNS axonal defects caused by loss of either gene alone Liebl et al. Although there is currently no biochemical evidence to support a direct interaction between Abl and Trio, the Abl pathway is a possible alternative to PAK activation in Trio signal transduction. MIG-2 seems to be a significant in vivo target for UNC signaling, because defects observed in weak loss-of-function unc mutants are enhanced by mutations in mig-2 and suppressed by increasing the genetic dose of mig-2 Zipkin et al.
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Genetic data from the Drosophila retina seem to preclude a role for Rho activation in Drosophila trio signaling, but other observations suggest that Rho-like proteins are involved. Furthermore, loss-of-function mutations in trio cause a dramatic overextension of neurites in the mushroom bodies of the developing brain, a phenotype observed in loss-of-function clones of rhoA Awasaki et al.