A death domain receptor signaling adaptor protein that plays a role in signaling the activation of INITIATOR CASPASES such as CASPASE 2. It contains a death domain that is specific for RIP SERINE-THEONINE KINASES and a caspase-binding domain that binds to and activates CASPASES such as CASPASE 2.
A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymes
A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. They perform functions such as binding to the cell membrane, capturing cargo molecules and promoting the assembly of CLATHRIN. The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found.
A signal transducing adaptor protein that links extracellular signals to the MAP KINASE SIGNALING SYSTEM. Grb2 associates with activated EPIDERMAL GROWTH FACTOR RECEPTOR and PLATELET-DERIVED GROWTH FACTOR RECEPTORS via its SH2 DOMAIN. It also binds to and translocates the SON OF SEVENLESS PROTEINS through its SH3 DOMAINS to activate PROTO-ONCOGENE PROTEIN P21(RAS).
A family of signaling adaptor proteins that contain SRC HOMOLOGY DOMAINS. Many members of this family are involved in transmitting signals from CELL SURFACE RECEPTORS to MITOGEN-ACTIVATED PROTEIN KINASES.
An adaptor protein complex primarily involved in the formation of clathrin-related endocytotic vesicles (ENDOSOMES) at the CELL MEMBRANE.
An adaptor protein complex found primarily on perinuclear compartments.
A clathrin adaptor protein complex primarily involved in clathrin-related transport at the TRANS-GOLGI NETWORK.

Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria. (1/30)

Caspase-2 is one of the earliest identified caspases, but the mechanism of caspase-2-induced apoptosis remains unknown. We show here that caspase-2 engages the mitochondria-dependent apoptotic pathway by inducing the release of cytochrome c (Cyt c) and other mitochondrial apoptogenic factors into the cell cytoplasm. In support of these observations we found that Bcl-2 and Bcl-xL can block caspase-2- and CRADD (caspase and RIP adaptor with death domain)-induced cell death. Unlike caspase-8, which can process all known caspase zymogens directly, caspase-2 is completely inactive toward other caspase zymogens. However, like caspase-8, physiological levels of purified caspase-2 can cleave cytosolic Bid protein, which in turn can trigger the release of Cyt c from isolated mitochondria. Interestingly, caspase-2 can also induce directly the release of Cyt c, AIF (apoptosis-inducing factor), and Smac (second mitochondria-derived activator of caspases protein) from isolated mitochondria independent of Bid or other cytosolic factors. The caspase-2-released Cyt c is sufficient to activate the Apaf-caspase-9 apoptosome in vitro. In combination, our data suggest that caspase-2 is a direct effector of the mitochondrial apoptotic pathway.  (+info)

Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5. (2/30)

BACKGROUND: The cyclic AMP specific phosphodiesterase, PDE4D5 interacts with the beta-propeller protein RACK1 to form a signaling scaffold complex in cells. Two-hybrid analysis of truncation and mutant constructs of the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5 were used to define a domain conferring interaction with the signaling scaffold protein, RACK1. RESULTS: Truncation and mutagenesis approaches showed that the RACK1-interacting domain on PDE4D5 comprised a cluster of residues provided by Asn-22/Pro-23/Trp-24/Asn-26 together with a series of hydrophobic amino acids, namely Leu-29, Val-30, Leu-33, Leu-37 and Leu-38 in a 'Leu-Xaa-Xaa-Xaa-Leu' repeat. This was done by 2-hybrid analyses and then confirmed in biochemical pull down analyses using GST-RACK1 and mutant PDE4D5 forms expressed in COS cells. Mutation of Arg-34, to alanine, in PDE4D5 attenuated its interaction with RACK1 both in 2-hybrid screens and in pull down analyses. A 38-mer peptide, whose sequence reflected residues 12 through 49 of PDE4D5, bound to RACK1 with similar affinity to native PDE4D5 itself (Ka circa 6 nM). CONCLUSIONS: The RACK1 Interaction Domain on PDE4D5, that we here call RAID1, is proposed to form an amphipathic helical structure that we suggest may interact with the C-terminal beta-propeller blades of RACK1 in a manner akin to the interaction of the helical G-gamma signal transducing protein with the beta-propeller protein, G-beta.  (+info)

RAIDD aggregation facilitates apoptotic death of PC12 cells and sympathetic neurons. (3/30)

In human cell lines, the caspase 2 adaptor RAIDD interacts selectively with caspase 2 through its caspase recruitment domain (CARD) and leads to caspase 2-dependent death. Whether RAIDD induces such effects in neuronal cells is unknown. We have previously shown that caspase 2 is essential for apoptosis of trophic factor-deprived PC12 cells and rat sympathetic neurons. We report here that rat RAIDD, cloned from PC12 cells, interacts with rat caspase 2 CARD. RAIDD overexpression induced caspase 2 CARD- and caspase 9-dependent apoptosis of PC12 cells and sympathetic neurons. Apoptosis correlated with the formation of discrete perinuclear aggregates. Both death and aggregates required the expression of full-length RAIDD. Such aggregates may enable more effective activation of caspase 2 through close proximity. Following trophic deprivation, RAIDD overexpression increased death and aggregate formation. Therefore, RAIDD aggregation is important for its death-promoting effects and may play a role in trophic factor withdrawal-induced neuronal apoptosis.  (+info)

The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. (4/30)

Apoptosis is triggered by activation of initiator caspases upon complex-mediated clustering of the inactive zymogen, as occurs in the caspase-9-activating apoptosome complex. Likewise, caspase-2, which is involved in stress-induced apoptosis, is recruited into a large protein complex, the molecular composition of which remains elusive. We show that activation of caspase-2 occurs in a complex that contains the death domain-containing protein PIDD, whose expression is induced by p53, and the adaptor protein RAIDD. Increased PIDD expression resulted in spontaneous activation of caspase-2 and sensitization to apoptosis by genotoxic stimuli. Because PIDD functions in p53-mediated apoptosis, the complex assembled by PIDD and caspase-2 is likely to regulate apoptosis induced by genotoxins.  (+info)

Association of caspase-2 with the promyelocytic leukemia protein nuclear bodies. (5/30)

Apoptotic cell death is executed by a family of cysteine proteases known as caspases. Synthesized as inactive precursors, caspases become activated sequentially in cascades. Activation of apical or initiator caspases in these cascades occurs in macromolecular complexes located in various compartments. One such complex is the plasma membrane-bound death-inducing signaling complex (DISC), formed upon engagement of death receptors, which recruits and activates caspase-8 and -10. Another complex is the cytosolic apoptosome, assembled in response to the release of mitochondrial cytochrome c, which recruits caspase-9. The other major human initiator caspase is caspase-2, which is activated in response to various lethal stimuli and has recently been shown to be required for DNA damage-induced apoptosis. The regulation of caspase-2 is not well understood. Here we present evidence that caspase-2 is localized to the promyelocytic leukemia protein nuclear bodies (PML-NBs), nuclear macro-molecular complexes that are involved in many scenarios of apoptosis including DNA damage. The localization of caspase-2 requires both the prodomain and protease domain but appears to be independent of its adaptor protein, CRADD/RAIDD. These data suggest the existence of a nuclear apoptosis pathway that involves both caspase-2 and the PML-NBs.  (+info)

RAIDD is required for apoptosis of PC12 cells and sympathetic neurons induced by trophic factor withdrawal. (6/30)

Caspase 2 has been implicated in trophic deprivation-induced neuronal death. We have shown that overexpression of the caspase 2-binding protein RAIDD induces neuronal apoptosis, acting synergistically with trophic deprivation. Currently, we examine the role of endogenous RAIDD in apoptosis of PC12 cells and sympathetic neurons. Expression of a truncated caspase recruitment domain-only form of caspase 2, which presumably disrupts the RAIDD interaction with endogenous caspase 2, attenuated trophic deprivation-induced apoptosis. Furthermore, downregulation of RAIDD by small interfering RNA led to inhibition of trophic deprivation-induced death, whereas death induced by DNA damage, which is not caspase 2-mediated, was not inhibited. Therefore, RAIDD, likely through interaction with caspase 2, is involved in trophic deprivation-induced neuronal apoptosis. This is the first demonstration of the involvement of RAIDD in apoptosis, and provides further support for the idea that apoptotic pathways in the same system may differ depending on the initiating stimulus.  (+info)

Apoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD. (7/30)

The p53 tumor suppressor promotes cell cycle arrest or apoptosis in response to diverse stress stimuli. p53-mediated cell death depends in large part on transcriptional up-regulation of target genes. One of these targets, P53-induced protein with a death domain (PIDD), was shown to function as a mediator of p53-dependent apoptosis. Here we show that PIDD is a cytoplasmic protein, and that PIDD-induced apoptosis and growth suppression in embryonic fibroblasts depend on the adaptor protein receptor-interacting protein (RIP)-associated ICH-1/CED-3 homologous protein with a death domain (RAIDD). We provide evidence that PIDD-induced cell death is associated with the early activation of caspase-2 and later activation of caspase-3 and -7. Our results also show that caspase-2(-/-), in contrast to RAIDD(-/-), mouse embryonic fibroblasts, are only partially resistant to PIDD. Our findings suggest that caspase-2 contributes to PIDD-mediated cell death, but that it is not the sole effector of this pathway.  (+info)

PIDD mediates NF-kappaB activation in response to DNA damage. (8/30)

Activation of NF-kappaB following genotoxic stress allows time for DNA-damage repair and ensures cell survival accounting for acquired chemoresistance, an impediment to effective cancer therapy. Despite this clinical relevance, little is known about pathways that enable genotoxic-stress-induced NF-kappaB induction. Previously, we reported a role for the p53-inducible death-domain-containing protein, PIDD, in caspase-2 activation and apoptosis in response to DNA damage. We now demonstrate that PIDD plays a critical role in DNA-damage-induced NF-kappaB activation. Upon genotoxic stress, a complex between PIDD, the kinase RIP1, and a component of the NF-kappaB-activating kinase complex, NEMO, is formed. PIDD expression enhances genotoxic-stress-induced NF-kappaB activation through augmented sumoylation and ubiquitination of NEMO. Depletion of PIDD and RIP1, but not caspase-2, abrogates DNA-damage-induced NEMO modification and NF-kappaB activation. We propose that PIDD acts as a molecular switch, controlling the balance between life and death upon DNA damage.  (+info)

CRADD, or Cav-1 related death domain protein, is a signaling adaptor protein that plays a role in regulating cell death and survival pathways. It contains a death domain that allows it to interact with other proteins involved in these pathways, including the tumor suppressor protein p53 and the death receptor Fas. CRADD has been implicated in a number of cellular processes, including apoptosis (programmed cell death), autophagy, and inflammation. Mutations in the CRADD gene have been associated with various diseases, including neurodevelopmental disorders and cancer.

Adaptor proteins are a type of protein that play a crucial role in intracellular signaling pathways by serving as a link between different components of the signaling complex. Specifically, "signal transducing adaptor proteins" refer to those adaptor proteins that are involved in signal transduction processes, where they help to transmit signals from the cell surface receptors to various intracellular effectors. These proteins typically contain modular domains that allow them to interact with multiple partners, thereby facilitating the formation of large signaling complexes and enabling the integration of signals from different pathways.

Signal transducing adaptor proteins can be classified into several families based on their structural features, including the Src homology 2 (SH2) domain, the Src homology 3 (SH3) domain, and the phosphotyrosine-binding (PTB) domain. These domains enable the adaptor proteins to recognize and bind to specific motifs on other signaling molecules, such as receptor tyrosine kinases, G protein-coupled receptors, and cytokine receptors.

One well-known example of a signal transducing adaptor protein is the growth factor receptor-bound protein 2 (Grb2), which contains an SH2 domain that binds to phosphotyrosine residues on activated receptor tyrosine kinases. Grb2 also contains an SH3 domain that interacts with proline-rich motifs on other signaling proteins, such as the guanine nucleotide exchange factor SOS. This interaction facilitates the activation of the Ras small GTPase and downstream signaling pathways involved in cell growth, differentiation, and survival.

Overall, signal transducing adaptor proteins play a critical role in regulating various cellular processes by modulating intracellular signaling pathways in response to extracellular stimuli. Dysregulation of these proteins has been implicated in various diseases, including cancer and inflammatory disorders.

Adaptor proteins play a crucial role in vesicular transport, which is the process by which materials are transported within cells in membrane-bound sacs called vesicles. These adaptor proteins serve as a bridge between vesicle membranes and cytoskeletal elements or other cellular structures, facilitating the movement of vesicles throughout the cell.

There are several different types of adaptor proteins involved in vesicular transport, each with specific functions and localizations within the cell. Some examples include:

1. Clathrin Adaptor Protein Complex (AP-1, AP-2, AP-3, AP-4): These complexes are responsible for recruiting clathrin to membranes during vesicle formation, which helps to shape and stabilize the vesicle. They also play a role in sorting cargo into specific vesicles.

2. Coat Protein Complex I (COPI): This complex is involved in the transport of proteins between the endoplasmic reticulum (ER) and the Golgi apparatus, as well as within the Golgi itself. COPI-coated vesicles are formed by the assembly of coatomer proteins around the membrane, which helps to deform the membrane into a vesicle shape.

3. Coat Protein Complex II (COPII): This complex is involved in the transport of proteins from the ER to the Golgi apparatus. COPII-coated vesicles are formed by the assembly of Sar1, Sec23/24, and Sec13/31 proteins around the membrane, which helps to select cargo and form a vesicle.

4. BAR (Bin/Amphiphysin/Rvs) Domain Proteins: These proteins are involved in shaping and stabilizing membranes during vesicle formation. They can sense and curve membranes, recruiting other proteins to help form the vesicle.

5. SNARE Proteins: While not strictly adaptor proteins, SNAREs play a critical role in vesicle fusion by forming complexes that bring the vesicle and target membrane together. These complexes provide the energy required for membrane fusion, allowing for the release of cargo into the target compartment.

Overall, adaptor proteins are essential components of the cellular machinery that regulates intracellular trafficking. They help to select cargo, deform membranes, and facilitate vesicle formation, ensuring that proteins and lipids reach their correct destinations within the cell.

The GRB2 (Growth Factor Receptor-Bound Protein 2) adaptor protein is a cytoplasmic signaling molecule that plays a crucial role in intracellular signal transduction pathways, particularly those involved in cell growth, differentiation, and survival. It acts as a molecular adapter or scaffold, facilitating the interaction between various proteins to form multi-protein complexes and propagate signals from activated receptor tyrosine kinases (RTKs) to downstream effectors.

GRB2 contains several functional domains, including an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The SH2 domain is responsible for binding to specific phosphotyrosine residues on activated RTKs or other adaptor proteins, while the SH3 domains mediate interactions with proline-rich sequences in partner proteins.

Once GRB2 binds to an activated RTK, it recruits and activates the guanine nucleotide exchange factor SOS (Son of Sevenless), which in turn activates the RAS GTPase. Activated RAS then initiates a signaling cascade involving various kinases such as Raf, MEK, and ERK, ultimately leading to changes in gene expression and cellular responses.

In summary, GRB2 is an essential adaptor protein that facilitates the transmission of signals from activated growth factor receptors to downstream effectors, playing a critical role in regulating various cellular processes.

SHC (Src homology 2 domain containing) signaling adaptor proteins are a family of intracellular signaling molecules that play a crucial role in the transduction of signals from various cell surface receptors, including receptor tyrosine kinases (RTKs). These proteins contain several conserved domains, including Src homology 2 (SH2) and phosphotyrosine-binding (PTB) domains, which enable them to bind to specific phosphorylated tyrosine residues on activated receptors or other signaling molecules.

Once bound to the activated receptor, SHC proteins recruit and interact with various downstream signaling proteins, such as growth factor receptor-bound protein 2 (Grb2) and son of sevenless (SOS), thereby initiating intracellular signaling cascades that ultimately regulate diverse cellular processes, including proliferation, differentiation, survival, and migration. There are three main isoforms of SHC proteins in humans: p66Shc, p52Shc, and p46Shc, which differ in their structural organization and functional properties.

Abnormal regulation of SHC signaling adaptor proteins has been implicated in various pathological conditions, including cancer, diabetes, and neurodegenerative diseases. Therefore, understanding the molecular mechanisms underlying SHC-mediated signaling pathways may provide valuable insights into the development of novel therapeutic strategies for these disorders.

Adaptor Protein Complex 2 (AP-2) is a protein complex that plays a crucial role in the formation of clathrin-coated vesicles, which are involved in intracellular trafficking and transport of membrane proteins and lipids. The AP-2 complex is composed of four subunits: alpha, beta, mu, and sigma, which form a heterotetrameric structure. It functions as a bridge between the clathrin lattice and the cytoplasmic domains of membrane proteins, such as transmembrane receptors, that are destined for endocytosis. The AP-2 complex recognizes specific sorting signals within the cytoplasmic tails of these membrane proteins, leading to their recruitment into forming clathrin-coated pits and subsequent internalization via clathrin-coated vesicles. This process is essential for various cellular functions, including receptor-mediated endocytosis, synaptic vesicle recycling, and membrane protein trafficking.

Adaptor Protein Complex 3 (APC3), also known as AP-3, is a type of adaptor protein complex that plays a crucial role in the sorting and trafficking of proteins within cells. It is composed of four subunits: delta, beta3A, mu3, and sigma3A. APC3 is primarily involved in the transport of proteins from the early endosomes to the lysosomes or to the plasma membrane. It also plays a role in the biogenesis of lysosome-related organelles such as melanosomes and platelet-dense granules. Mutations in the genes encoding for APC3 subunits have been associated with several genetic disorders, including Hermansky-Pudlak syndrome and Chediak-Higashi syndrome.

Adaptor Protein Complex 1 (AP-1) is a group of proteins that function as a complex to play a crucial role in the intracellular transport of various molecules, particularly in the formation of vesicles that transport cargo from one compartment of the cell to another. The AP-1 complex is composed of four subunits: γ, β1, μ1, and σ1. It is primarily associated with the trans-Golgi network and early endosomes, where it facilitates the sorting and packaging of cargo into vesicles for transport to various destinations within the cell. The AP-1 complex recognizes specific sorting signals on the membrane proteins and adaptor proteins, thereby ensuring the accurate delivery of cargo to the correct location. Defects in the AP-1 complex have been implicated in several human diseases, including neurological disorders and cancer.

Mitochondrial antiviral-signaling protein also known as CARD adapter inducing interferon-beta (Cardif/IPS-1) [13] CRADD: ... The adaptor protein VISA further activates the inhibitor of nuclear factor kappa-B kinase (IKK)-protein-kinase family members. ... Death adaptor molecule RAIDD-2 [15] RIG-I: Retinoic acid-inducible gene 1 protein, also known as DEAD-box protein 58 (DDX58) [ ... CARDs are found on a strikingly wide range of proteins, including helicases, kinases, mitochondrial proteins, caspases, and ...
To activate IKK, TAB2 and TAB3 adaptor proteins recruit TAK1 or MEKK3, which phosphorylate the complex. This results in the ... Distinct domains for nuclear factor-kappaB activation and association with tumor necrosis factor signaling proteins". The ... Ahmad M, Srinivasula SM, Wang L, Talanian RV, Litwack G, Fernandes-Alnemri T, Alnemri ES (February 1997). "CRADD, a novel human ... Chen D, Li X, Zhai Z, Shu HB (May 2002). "A novel zinc finger protein interacts with receptor-interacting protein (RIP) and ...
Lin Q, Liu Y, Moore DJ, Elizer SK, Veach RA, Hawiger J, Ruley HE (2012). "Cutting edge: the "death" adaptor CRADD/RAIDD targets ... which are thought to function as upstream regulators in NF-κB signaling. This protein is found to form a complex with the ... This protein is reported to interact with other CARD and coiled coil domain containing proteins including CARD9, -10, -11 and - ... "c-E10 is a caspase-recruiting domain-containing protein that interacts with components of death receptors signaling pathway and ...
... CASP2 and RIPK1 domain containing adaptor with death domain". Tinel A, Tschopp J (May 2004). "The PIDDosome, a protein ... Through its CARD domain, this protein interacts with, and thus recruits, caspase 2/ICH1 to the cell death signal transduction ... Death domain-containing protein CRADD is a protein that in humans is encoded by the CRADD gene. The protein encoded by this ... Human CRADD genome location and CRADD gene details page in the UCSC Genome Browser. Lennon G, Auffray C, Polymeropoulos M, ...
Mitochondrial antiviral-signaling protein also known as CARD adapter inducing interferon-beta (Cardif/IPS-1) [13] CRADD: ... The adaptor protein VISA further activates the inhibitor of nuclear factor kappa-B kinase (IKK)-protein-kinase family members. ... Death adaptor molecule RAIDD-2 [15] RIG-I: Retinoic acid-inducible gene 1 protein, also known as DEAD-box protein 58 (DDX58) [ ... CARDs are found on a strikingly wide range of proteins, including helicases, kinases, mitochondrial proteins, caspases, and ...
CRADD Signaling Adaptor Protein D12.644.360.24.296.50 D12.644.360.24.285.50 D12.776.157.57.04.186 D12.776.157.57.06.186 CREB- ... GRB2 Adaptor Protein D12.644.360.24.297 D12.644.360.24.290 GRB7 Adaptor Protein D12.644.360.24.298 D12.644.360.24.299 Great ... Nod Signaling Adaptor Proteins D12.644.360.24.307 D12.644.360.24.313 D12.776.157.57.68 D12.644.360.539.500 D12.776.157.57.78 ... Nod1 Signaling Adaptor Protein D12.644.360.24.307.249 D12.644.360.24.313.249 D12.776.157.57.04.249 D12.644.360.539.500.249 ...
CRADD Signaling Adaptor Protein D12.644.360.24.296.50 D12.644.360.24.285.50 D12.776.157.57.04.186 D12.776.157.57.06.186 CREB- ... GRB2 Adaptor Protein D12.644.360.24.297 D12.644.360.24.290 GRB7 Adaptor Protein D12.644.360.24.298 D12.644.360.24.299 Great ... Nod Signaling Adaptor Proteins D12.644.360.24.307 D12.644.360.24.313 D12.776.157.57.68 D12.644.360.539.500 D12.776.157.57.78 ... Nod1 Signaling Adaptor Protein D12.644.360.24.307.249 D12.644.360.24.313.249 D12.776.157.57.04.249 D12.644.360.539.500.249 ...
CRADD Signaling Adaptor Protein. *Edar-Associated Death Domain Protein. *Fas-Associated Death Domain Protein ... Adaptor Proteins, Signal Transducing [D12.644.360.024]. *Death Domain Receptor Signaling Adaptor Proteins [D12.644.360.024.296] ... Adaptor Proteins, Signal Transducing [D12.776.157.057]. *Death Domain Receptor Signaling Adaptor Proteins [D12.776.157.057.024] ... Adaptor Proteins, Signal Transducing [D12.776.476.024]. *Death Domain Receptor Signaling Adaptor Proteins [D12.776.476.024.375] ...
CRADD Signaling Adaptor Protein. Proteína Adaptadora de Sinalização CRADD. Proteína Adaptadora de Señalización CRADD. ... Death Domain Receptor Signaling Adaptor Proteins. Proteínas Adaptadoras de Sinalização de Receptores de Domínio de Morte. ... CARD Signaling Adaptor Proteins. Proteínas Adaptadoras de Sinalização CARD. Proteínas Adaptadoras de Señalización CARD. ... Nod Signaling Adaptor Proteins. Proteínas Adaptadoras de Sinalização Nod. Proteínas Adaptadoras de Señalización Nod. ...
It shows genes and PPIs with information about pathways, protein-protein interactions (PPIs), Gene Ontology (GO) annotations ... a web resource for human protein-protein interactions. ... Regulation Of Rab Protein Signal Transduction. *Regulation Of ... Protein-Protein Interactions. 11 interactors: APPL1 CRADD MTA2 POT1 RAB22A RAB5A RAB5C RBBP7 RUVBL2 SUV39H2 TINF2 41 ... adaptor protein, phosphotyrosine interaction, PH domain and leucine zipper containing 2. RAB5A, member RAS oncogene family. ...
... are reported to be caused by recessive variants in CRADD. Among five families of different ethnicities identified, one ... CRADD Signaling Adaptor Protein / genetics* Actions. * Search in PubMed * Search in MeSH ... Homozygous null variant in CRADD, encoding an adaptor protein that mediates apoptosis, is associated with lissencephaly. Harel ... Mutations in CRADD Result in Reduced Caspase-2-Mediated Neuronal Apoptosis and Cause Megalencephaly with a Rare Lissencephaly ...
CRADD Signaling Adaptor Protein D12.644.360.24.296.50 D12.644.360.24.285.50 D12.776.157.57.04.186 D12.776.157.57.06.186 CREB- ... GRB2 Adaptor Protein D12.644.360.24.297 D12.644.360.24.290 GRB7 Adaptor Protein D12.644.360.24.298 D12.644.360.24.299 Great ... Nod Signaling Adaptor Proteins D12.644.360.24.307 D12.644.360.24.313 D12.776.157.57.68 D12.644.360.539.500 D12.776.157.57.78 ... Nod1 Signaling Adaptor Protein D12.644.360.24.307.249 D12.644.360.24.313.249 D12.776.157.57.04.249 D12.644.360.539.500.249 ...
CASP8 and FADD-Like Apoptosis Regulating Protein [D12.644.360.024.285.024] * CRADD Signaling Adaptor Protein [D12.644.360.024. ... Carrier Proteins [D12.776.157] * Adaptor Proteins, Signal Transducing [D12.776.157.057] * CARD Signaling Adaptor Proteins [ ... Amino Acids, Peptides, and Proteins [D12] * Proteins [D12.776] * Carrier Proteins [D12.776.157] * Adaptor Proteins, Signal ... Amino Acids, Peptides, and Proteins [D12] * Proteins [D12.776] * Carrier Proteins [D12.776.157] * Adaptor Proteins, Signal ...
CASP8 and FADD-Like Apoptosis Regulating Protein [D12.644.360.024.285.024] * CRADD Signaling Adaptor Protein [D12.644.360.024. ... Carrier Proteins [D12.776.157] * Adaptor Proteins, Signal Transducing [D12.776.157.057] * CARD Signaling Adaptor Proteins [ ... Amino Acids, Peptides, and Proteins [D12] * Proteins [D12.776] * Carrier Proteins [D12.776.157] * Adaptor Proteins, Signal ... Amino Acids, Peptides, and Proteins [D12] * Proteins [D12.776] * Carrier Proteins [D12.776.157] * Adaptor Proteins, Signal ...
CRADD Signaling Adaptor Protein Entry term(s). Caspase and Rip Adaptor with Death Domain Protein RAIDD Signaling Adaptor ... CRADD Signaling Adaptor Protein - Preferred Concept UI. M0492988. Scope note. A death domain receptor signaling adaptor protein ... Caspase and Rip Adaptor with Death Domain Protein. RAIDD Signaling Adaptor Protein. RIP Associated Protein With a Death Domain ... A death domain receptor signaling adaptor protein that plays a role in signaling the activation of INITIATOR CASPASES such as ...
CRADD Signaling Adaptor Protein D12.644.360.24.296.50 D12.644.360.24.285.50 D12.776.157.57.04.186 D12.776.157.57.06.186 CREB- ... GRB2 Adaptor Protein D12.644.360.24.297 D12.644.360.24.290 GRB7 Adaptor Protein D12.644.360.24.298 D12.644.360.24.299 Great ... Nod Signaling Adaptor Proteins D12.644.360.24.307 D12.644.360.24.313 D12.776.157.57.68 D12.644.360.539.500 D12.776.157.57.78 ... Nod1 Signaling Adaptor Protein D12.644.360.24.307.249 D12.644.360.24.313.249 D12.776.157.57.04.249 D12.644.360.539.500.249 ...
This gene encodes a protein containing a death domain (DD) motif. This protein recruits caspase 2/ICH1 to the cell death signal ... Also recruits CASP2 to the TNFR-1 signaling complex through its interaction with RIPK1 and TRADD and may play a role in the ... Adapter protein that associates with PIDD1 and the caspase CASP2 to form the PIDDosome, a complex that activates CASP2 and ... Adapter protein that associates with PIDD1 and the caspase CASP2 to form the PIDDosome, a complex that activates CASP2 and ...
Factor II N0000170109 COUP Transcription Factors N0000166993 Crack Cocaine N0000175212 CRADD Signaling Adaptor Protein ... Nod Signaling Adaptor Proteins N0000175216 Nod1 Signaling Adaptor Protein N0000175217 Nod2 Signaling Adaptor Protein ... GRB10 Adaptor Protein N0000170457 GRB2 Adaptor Protein N0000170455 GRB7 Adaptor Protein N0000169111 Green Fluorescent Proteins ... Adaptor Protein Complex 1 N0000168711 Adaptor Protein Complex 2 N0000168710 Adaptor Protein Complex 3 N0000168702 Adaptor ...
The adaptor CRADD/RAIDD controls activation of endothelial cells by proinflammatory stimuli.. Qiao H; Liu Y; Veach RA; ... Targeting Non-proteolytic Protein Ubiquitination for the Treatment of Diffuse Large B Cell Lymphoma.. Yang Y; Kelly P; Shaffer ... 7. AIP augments CARMA1-BCL10-MALT1 complex formation to facilitate NF-κB signaling upon T cell activation.. Schimmack G; ... The protein kinase C-responsive inhibitory domain of CARD11 functions in NF-kappaB activation to regulate the association of ...
CRADD Signaling Adaptor Protein Crambe Plant Crambe Sponge Crangonidae Cranial Fontanelles Cranial Fossa, Anterior Cranial ... Adaptor Protein Complex 1 Adaptor Protein Complex 2 Adaptor Protein Complex 3 Adaptor Protein Complex 4 Adaptor Protein Complex ... Adaptor Protein Complex sigma Subunits Adaptor Protein Complex Subunits Adaptor Proteins, Signal Transducing Adaptor Proteins, ... Adaptor Protein Complex beta Subunits Adaptor Protein Complex delta Subunits Adaptor Protein Complex gamma Subunits Adaptor ...
... or as an apoptosis-inducing protein by activating caspase-2. Biallelic truncating mutations in CRADD-the protein bridging PIDD1 ... Mutations in adaptor protein complex-4 (AP-4) genes have first been identified in 2009, causing a phenotype termed as AP-4 ... Genetic alterations in cilia, highly-conserved organelles with sensorineural and signal transduction roles can compromise their ... Proteína Adaptadora de Sinalização CRADD , Deficiência Intelectual , Animais , Proteína Adaptadora de Sinalização CRADD/ ...
It shows genes and PPIs with information about pathways, protein-protein interactions (PPIs), Gene Ontology (GO) annotations ... a web resource for human protein-protein interactions. ... Gastrin-CREB signalling pathway via PKC and MAPK. *Response to ... CRADD CRHR2 CRIP2 CRYAB CSAG1 CSNK1D CSNK1E CSNK1G1 CSNK1G2 CSNK2A1 CSRP1 CST2 CSTF2 CTBP2 CTF1 CTNNA1 CTNNB1 CTNND1 CTSB CTSD ... Protein-Protein Interactions. 1995 interactors: A2M AAK1 AAMDC ABCB7 ABCF1 ABHD10 ABHD11 ABL1 ABLIM1 ABR ACAA2 ACAD10 ACAD11 ...
  • Upon activation of Ipaf-1 by the intracellular bacterium S. typhimurium or other stress signals, Ipaf-1 recruits a CARD-containing adapter termed ASC and caspase-1 in unknown stoichiometry via CARD-CARD association. (wikipedia.org)
  • Recently, a subset of CARD-containing proteins has been shown to participate in recognition of intracellular double-stranded RNA, a common constituent of a number of viral genomes, including the para- and orthomyxoviridae and rhabdoviridae. (wikipedia.org)
  • Gain-of-function mutations in the intracellular NOD2 protein has been linked to increased risk for Crohn's disease. (wikipedia.org)
  • Intracellular signaling adaptor proteins that bind to the cytoplasmic death domain region found on DEATH DOMAIN RECEPTORS. (uams.edu)
  • Many of the proteins in this class take part in intracellular signaling from TUMOR NECROSIS FACTOR RECEPTORS. (uams.edu)
  • These domains mediate the formation of larger protein complexes via direct interactions between individual CARDs. (wikipedia.org)
  • 2006). Various studies have also demonstrated the involvement of several other signaling components in virus-induced activation of NF-κB and/or IRF3, including TRAF3, TRAF6, TANK, NEMO (IKKg), TRADD, FADD, and RIP (Kawai et al. (wikipedia.org)
  • Death Domain Receptor Signaling Adaptor Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uams.edu)
  • This graph shows the total number of publications written about "Death Domain Receptor Signaling Adaptor Proteins" by people in UAMS Profiles by year, and whether "Death Domain Receptor Signaling Adaptor Proteins" was a major or minor topic of these publications. (uams.edu)
  • Below are the most recent publications written about "Death Domain Receptor Signaling Adaptor Proteins" by people in Profiles over the past ten years. (uams.edu)
  • CARDs are a subclass of protein motif known as the death fold, which features an arrangement of six to seven antiparallel alpha helices with a hydrophobic core and an outer face composed of charged residues. (wikipedia.org)
  • Caspase recruitment domains, or caspase activation and recruitment domains (CARDs), are interaction motifs found in a wide array of proteins, typically those involved in processes relating to inflammation and apoptosis. (wikipedia.org)
  • A death domain receptor signaling adaptor protein that plays a role in signaling the activation of INITIATOR CASPASES such as CASPASE 2 . (nih.gov)
  • Adapter protein that associates with PIDD1 and the caspase CASP2 to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis (PubMed:9044836, PubMed:15073321, PubMed:16652156, PubMed:17159900, PubMed:17289572). (nih.gov)
  • This protein recruits caspase 2/ICH1 to the cell death signal transduction complex, which includes tumor necrosis factor receptor 1 (TNFR1A) and RIPK1/RIP kinase, and acts in promoting apoptosis. (nih.gov)
  • Also recruits CASP2 to the TNFR-1 signaling complex through its interaction with RIPK1 and TRADD and may play a role in the tumor necrosis factor-mediated signaling pathway (PubMed:8985253). (nih.gov)
  • 11. Ancient Origin of the CARD-Coiled Coil/Bcl10/MALT1-Like Paracaspase Signaling Complex Indicates Unknown Critical Functions. (nih.gov)
  • Chromatin immunoprecipitation-sequencing revealed binding of wild-type ZBTB11 to promoters in 238 genes, among which genes encoding proteins involved in mitochondrial functions and RNA processing are over-represented. (bvsalud.org)
  • 7. AIP augments CARMA1-BCL10-MALT1 complex formation to facilitate NF-κB signaling upon T cell activation. (nih.gov)
  • 16. The adaptor CRADD/RAIDD controls activation of endothelial cells by proinflammatory stimuli. (nih.gov)
  • 18. Malt1 ubiquitination triggers NF-kappaB signaling upon T-cell activation. (nih.gov)