Armadillo Domain Proteins
Armadillos
Xenarthra
Wnt1 Protein
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Sequence Homology, Amino Acid
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Mycobacterium leprae
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alpha Catenin
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Uridine Phosphorylase
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Membrane-tethered Drosophila Armadillo cannot transduce Wingless signal on its own. (1/286)
Drosophila Armadillo and its vertebrate homolog beta-catenin are key effectors of Wingless/Wnt signaling. In the current model, Wingless/Wnt signal stabilizes Armadillo/beta-catenin, which then accumulates in nuclei and binds TCF/LEF family proteins, forming bipartite transcription factors which activate transcription of Wingless/Wnt responsive genes. This model was recently challenged. Overexpression in Xenopus of membrane-tethered beta-catenin or its paralog plakoglobin activates Wnt signaling, suggesting that nuclear localization of Armadillo/beta-catenin is not essential for signaling. Tethered plakoglobin or beta-catenin might signal on their own or might act indirectly by elevating levels of endogenous beta-catenin. We tested these hypotheses in Drosophila by removing endogenous Armadillo. We generated a series of mutant Armadillo proteins with altered intracellular localizations, and expressed these in wild-type and armadillo mutant backgrounds. We found that membrane-tethered Armadillo cannot signal on its own; however it can function in adherens junctions. We also created mutant forms of Armadillo carrying heterologous nuclear localization or nuclear export signals. Although these signals alter the subcellular localization of Arm when overexpressed in Xenopus, in Drosophila they have little effect on localization and only subtle effects on signaling. This supports a model in which Armadillo's nuclear localization is key for signaling, but in which Armadillo intracellular localization is controlled by the availability and affinity of its binding partners. (+info)Negative regulation of Wingless signaling by D-axin, a Drosophila homolog of axin. (2/286)
Wnt/Wingless directs many cell fates during development. Wnt/Wingless signaling increases the amount of beta-catenin/Armadillo, which in turn activates gene transcription. Here the Drosophila protein D-Axin was shown to interact with Armadillo and D-APC. Mutation of d-axin resulted in the accumulation of cytoplasmic Armadillo and one of the Wingless target gene products, Distal-less. Ectopic expression of d-axin inhibited Wingless signaling. Hence, D-Axin negatively regulates Wingless signaling by down-regulating the level of Armadillo. These results establish the importance of the Axin family of proteins in Wnt/Wingless signaling in Drosophila. (+info)The ciD mutation encodes a chimeric protein whose activity is regulated by Wingless signaling. (3/286)
The Drosophila cubitus interruptus (ci) gene encodes a sequence-specific DNA-binding protein that regulates transcription of Hedgehog (Hh) target genes. Activity of the Ci protein is posttranslationally regulated by Hh signaling. In animals homozygous for the ciD mutation, however, transcription of Hh target genes is regulated by Wingless (Wg) signaling rather than by Hh signaling. We show that ciD encodes a chimeric protein composed of the regulatory domain of dTCF/Pangolin (Pan) and the DNA binding domain of Ci. Pan is a Wg-regulated transcription factor that is activated by binding of Armadillo (Arm) to its regulatory domain. Arm is thought to activate Pan by contributing a transactivation domain. We find that a constitutively active form of Arm potentiates activity of a CiD transgene and coimmunoprecipitates with CiD protein. The Wg-responsive activity of CiD could be explained by recruitment of the Arm transactivation function to the promoters of Hh-target genes. We suggest that wild-type Ci also recruits a protein with a transactivation domain as part of its normal mechanism of activation. (+info)The C-terminal domain of armadillo binds to hypophosphorylated teashirt to modulate wingless signalling in Drosophila. (4/286)
Wnt signalling is a key pathway for tissue patterning during animal development. In Drosophila, the Wnt protein Wingless acts to stabilize Armadillo inside cells where it binds to at least two DNA-binding factors which regulate specific target genes. One Armadillo-binding protein in Drosophila is the zinc finger protein Teashirt. Here we show that Wingless signalling promotes the phosphorylation and the nuclear accumulation of Teashirt. This process requires the binding of Teashirt to the C-terminal end of Armadillo. Finally, we present evidence that the serine/threonine kinase Shaggy is associated with Teashirt in a complex. We discuss these results with respect to current models of Armadillo/beta-catenin action for the transmission of the Wingless/Wnt pathway. (+info)Functional characterization of multiple transactivating elements in beta-catenin, some of which interact with the TATA-binding protein in vitro. (5/286)
beta-Catenin, a member of the family of Armadillo repeat proteins, plays a dual role in cadherin-mediated cell adhesion and in signaling by Wnt growth factors. Upon Wnt stimulation beta-catenin undergoes nuclear translocation and serves as transcriptional coactivator of T cell factor DNA-binding proteins. Previously the transactivation potential of different portions of beta-catenin has been demonstrated, but the precise location of transactivating elements has not been established. Also, the mechanism of transactivation by beta-catenin and the molecular basis for functional differences between beta-catenin and the closely related proteins Armadillo and Plakoglobin are poorly understood. Here we have used a yeast system for the detailed characterization of the transactivation properties of beta-catenin. We show that its transactivation domains possess a modular structure, consist of multiple subelements that cover broad regions at its N and C termini, and extend considerably into the Armadillo repeat region. Compared with beta-catenin the N termini of Plakoglobin and Armadillo have different transactivation capacities that may explain their distinct signaling properties. Furthermore, transactivating elements of beta-catenin interact specifically and directly with the TATA-binding protein in vitro providing further evidence that a major function of beta-catenin during Wnt signaling is to recruit the basal transcription machinery to promoter regions of Wnt target genes. (+info)A Drosophila Axin homolog, Daxin, inhibits Wnt signaling. (6/286)
The vertebrate Axin protein, the product of the mouse fused gene, binds to beta-catenin to inhibit Wnt signaling. We have identified a homolog of Axin in Drosophila, Daxin. Using double-stranded RNA interference, we generated loss-of-function phenotypes that are similar to overexpression of the Drosophila Wnt gene wingless (wg). Overexpression of Daxin produces phenotypes similar to loss of wg. In addition, we show that Daxin overexpression can modify phenotypes elicited by wg and another Drosophila Wnt gene, DWnt-2. Using immunoprecipitation of endogenous Daxin protein from embryos we show that Daxin interacts with Armadillo and Zeste-white 3. The loss-of-function and overexpression phenotypes show that Daxin, like its mammalian counterpart, acts as a negative regulator of wg/Wnt signaling. (+info)Frizzled and Dfrizzled-2 function as redundant receptors for Wingless during Drosophila embryonic development. (7/286)
In cell culture assays, Frizzled and Dfrizzled2, two members of the Frizzled family of integral membrane proteins, are able to bind Wingless and transduce the Wingless signal. To address the role of these proteins in the intact organism and to explore the question of specificity of ligand-receptor interactions in vivo, we have conducted a genetic analysis of frizzled and Dfrizzled2 in the embryo. These experiments utilize a small gamma-ray-induced deficiency that uncovers Dfrizzled2. Mutants lacking maternal frizzled and zygotic frizzled and Dfrizzled2 exhibit defects in the embryonic epidermis, CNS, heart and midgut that are indistinguishable from those observed in wingless mutants. Epidermal patterning defects in the frizzled, Dfrizzled2 double-mutant embryos can be rescued by ectopic expression of either gene. In frizzled, Dfrizzled2 mutant embryos, ectopic production of Wingless does not detectably alter the epidermal patterning defect, but ectopic production of an activated form of Armadillo produces a naked cuticle phenotype indistinguishable from that produced by ectopic production of activated Armadillo in wild-type embryos. These experiments indicate that frizzled and Dfrizzled2 function downstream of wingless and upstream of armadillo, consistent with their proposed roles as Wingless receptors. The lack of an effect on epidermal patterning of ectopic Wingless in a frizzled, Dfrizzled2 double mutant argues against the existence of additional Wingless receptors in the embryo or a model in which Frizzled and Dfrizzled2 act simply to present the ligand to its bona fide receptor. These data lead to the conclusion that Frizzled and Dfrizzled2 function as redundant Wingless receptors in multiple embryonic tissues and that this role is accurately reflected in tissue culture experiments. The redundancy of Frizzled and Dfrizzled2 explains why Wingless receptors were not identified in earlier genetic screens for mutants defective in embryonic patterning. (+info)Roles of the C terminus of Armadillo in Wingless signaling in Drosophila. (8/286)
Drosophila melanogaster Armadillo and its vertebrate homolog beta-catenin play multiple roles during development. Both are components of cell-cell adherens junctions and both transduce Wingless (Wg)/Wnt intercellular signals. The current model for Wingless signaling proposes that Armadillo binds the DNA-binding protein dTCF, forming a bipartite transcription factor that activates Wingless-responsive genes. In this model, Armadillo's C-terminal domain is proposed to serve an essential role as a transcriptional activation domain. In Xenopus, however, overexpression of C-terminally truncated beta-catenin activates Wnt signaling, suggesting that the C-terminal domain might not be essential. We reexamined the function of Armadillo's C terminus in Wingless signaling. We found that C-terminally truncated mutant Armadillo has a deficit in Wg-signaling activity, even when corrected for reduced protein levels. However, we also found that Armadillo proteins lacking all or part of the C terminus retain some signaling ability if overexpressed, and that mutants lacking different portions of the C-terminal domain differ in their level of signaling ability. Finally, we found that the C terminus plays a role in Armadillo protein stability in response to Wingless signal and that the C-terminal domain can physically interact with the Arm repeat region. These data suggest that the C-terminal domain plays a complex role in Wingless signaling and that Armadillo recruits the transcriptional machinery via multiple contact sites, which act in an additive fashion. (+info)Leprosy can cause a range of symptoms, including:
1. Skin lesions: Leprosy can cause skin lesions, including lighter or darker patches on the skin, and thickening of the skin.
2. Nerve damage: The bacteria can damage the nerves, leading to numbness, pain, and muscle weakness.
3. Eye problems: Leprosy can cause eye inflammation, vision loss, and dryness of the eyes.
4. Respiratory problems: In severe cases, leprosy can cause breathing difficulties and respiratory failure.
5. Enlarged lymph nodes: The lymph nodes may become enlarged in some cases.
6. Joint pain and swelling: Leprosy can cause joint pain and swelling.
7. Neuritis: Inflammation of the nerves can occur, leading to pain, numbness, and tingling sensations.
8. Ulcers: Leprosy can cause ulcers on the skin and mucous membranes.
Leprosy is diagnosed through a combination of physical examination, laboratory tests, and medical imaging. Treatment typically involves a combination of antibiotics and other medications to manage symptoms. In some cases, surgery may be necessary to remove infected tissue or repair damaged nerves.
Leprosy can be transmitted through respiratory droplets, close contact with an infected person, or through contaminated objects such as clothing or bedding. However, leprosy is not highly contagious and the risk of transmission is low if proper precautions are taken.
While there is no cure for leprosy, early diagnosis and treatment can prevent complications and disability. However, due to the stigma surrounding the disease, many people may delay seeking medical attention, leading to a higher risk of long-term complications.
Overall, while leprosy is a serious disease, it is also a preventable and treatable one. With proper awareness and education, we can work towards reducing the stigma surrounding leprosy and ensuring that those affected receive the medical attention they need.
Adhesome
Plakophilin-2
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Amino Acids1
- LRRK2 is a large multidomain protein with 2,527 amino acids (MW: 286 kDa) and consists of armadillo repeats (ARM), ankyrin repeats (ANK), leucine-rich repeats (LRR), Ras of complex (ROC), C-terminal of ROC (COR), kinase domain (KD), and WD40 domain. (wuxibiortus.com)
Drosophila2
- A family of proteins that contain several 42-amino acid repeat domains and are homologous to the Drosophila armadillo protein. (nih.gov)
- Familia de proteínas que contienen varios dominios de repetición de 42 aminioácidos y son homólogas a la proteína armadillo de Drosophila. (bvsalud.org)
Repeats3
- The structure of the ARMC5 protein contains ARM repeats and a BT. (endocrine-abstracts.org)
- Expanded CAG TRINUCLEOTIDE REPEATS have been identified in the Huntingtin (HD) Gene of patients with HUNTINGTON DISEASE and are associated with abnormal PROTEIN AGGREGATES . (nih.gov)
- The protein encoded by this gene contains 9 'Armadillo' repeats and interacts with the smg GDS protein through these repeats. (nih.gov)
ARMC52
- Background: Germline mutations of ARMC5 (Armadillo repeat containing 5 gene) were identified as a frequent cause of primary bilateral macronodular adrenal hyperplasia (PBMAH). (endocrine-abstracts.org)
- Background: ARMC5 (armadillo repeat containing 5) has been identified as the gene responsible for PBMAH (Primary Bilateral Macronodular Adrenal Hyperplasia). (endocrine-abstracts.org)
WD403
- 12. WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A. (nih.gov)
- They are large multi-domain proteins containing two putative catalytic domains, a GTPase ROCO domain and a kinase domain, in addition to armadillo, ankyrin, leucin rich and WD40 domains. (nih.gov)
- WD40 repeat-containing protein [Rivularia sp. (gzybioinformatics.cn)
Interpro1
- No InterPro domain matches or not analyzed. (cornell.edu)
Interacts1
- Interacts with the DNA-binding domain of p53/TP53. (cansar.ai)
Binds7
- 5. Intrinsically disordered protein NUPR1 binds to the armadillo-repeat domain of Plakophilin 1. (nih.gov)
- 10. The armadillo-repeat domain of plakophilin 1 binds the C-terminal sterile alpha motif (SAM) of p73. (nih.gov)
- 2. Protein phosphatase 2a (PP2A) binds within the oligomerization domain of striatin and regulates the phosphorylation and activation of the mammalian Ste20-Like kinase Mst3. (nih.gov)
- 4. Striatins contain a noncanonical coiled coil that binds protein phosphatase 2A A subunit to form a 2:2 heterotetrameric core of striatin-interacting phosphatase and kinase (STRIPAK) complex. (nih.gov)
- Arp2-3 complex binds WASP PROTEIN and existing ACTIN FILAMENTS, and it nucleates the formation of new branch point filaments. (nih.gov)
- HN - 2006 BX - Arp2-3 Complex MH - Actin-Related Protein 3 UI - D051378 MN - D5.750.78.730.246.750 MN - D12.776.220.525.246.750 MS - A component of the Arp2-3 complex that is related in sequence and structure to ACTIN and that binds ATP. (nih.gov)
- Binds to the tail domain of the KIF3A/KIF3B heterodimer to form a heterotrimeric KIF3 complex and may regulate the membrane binding of this complex (By similarity). (nih.gov)
Gene2
Helical1
- β-catenin contacts a disordered FOXP2 region with α-helical propensity via its folded armadillo domain, whereas the intrinsically disordered β-catenin N terminus and C terminus bind to the conserved FOXP2 DNA-binding domain. (medunigraz.at)
Putative1
- Cloning of the chicken and quail genes encoding the putative receptor for RSV, subgroup A. Although the sequencing of genes encoding this long-sought receptor is not yet complete, it will undoubtedly offer a new perspective on viral-host interactions, the mechanism of early events in the virus life cycle, and the nature of the presumptively polymorphic avian proteins that recognize the several subgroups of RSV. (nih.gov)
PFAM1
- This is a PFAM domain. (embl.de)
Motif1
- Sterile alpha and heat/Armadillo motif 1 (SARM1) is a protein expressed in neurons of the brain that plays a critical role in axonal degeneration. (nih.gov)
Cullin1
- This list was created primarily from Supplemental Table 1 of Li et al , with the addition of the Cullin proteins. (nih.gov)
Transmembrane protein1
- Demonstration that an ectopically expressed transmembrane protein (human CD4) can be efficiently incorporated into RSV envelopes during virus assembly (8). (nih.gov)
Bind3
- 7. Plakophilins 1 and 3 bind to FXR1 and thereby influence the mRNA stability of desmosomal proteins. (nih.gov)
- They bind to other proteins through their armadillo domains and play a variety of roles in the CELL including SIGNAL TRANSDUCTION , regulation of DESMOSOME assembly, and CELL ADHESION . (nih.gov)
- AN - coordinate IM with ADENOMA (IM) HN - 2006 BX - Corticotroph Adenoma BX - Pituitary Adenoma, ACTH-Secreting BX - Pituitary Corticotropin-Secreting Adenoma MH - Actin Capping Proteins UI - D051344 MN - D5.750.78.730.32 MN - D12.776.220.525.32 MS - Actin capping proteins are cytoskeletal proteins that bind to the ends of ACTIN FILAMENTS to regulate actin polymerization. (nih.gov)
Residues1
- 3. Several recent publications indicate the presence of a 'hydrophobic spine' formed by four conserved interacting hydrophobic residues in the kinase domain of SFKs. (edu.au)
Oncogenic2
Phosphatase2
- 3. A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein. (nih.gov)
- 15. Striatin-1 is a B subunit of protein phosphatase PP2A that regulates dendritic arborization and spine development in striatal neurons. (nih.gov)
Cellular3
- Protein kinases regulate almost every aspect of cellular function through phosphorylation of their substrates. (nih.gov)
- In addition to phosphorylating SFKs, CHK also performs non-SFK-related functions by phosphorylating other cellular protein substrates. (edu.au)
- Besides β-synuclein, cellular proteins containing motifs resembling this sequence are potential CHK substrates. (edu.au)
Transcription factor1
- The transcription factor forkhead box protein P2 (FOXP2) is a highly conserved key regulator of embryonal development. (medunigraz.at)
Repeat3
- LRRK1 is slightly smaller than LRRK2 due to the lack of an N-terminal armadillo repeat domain. (nih.gov)
- Kelch repeat type 1-containing protein [Acidovorax avenae subsp. (gzybioinformatics.cn)
- WD-40 repeat-containing protein [Roseiflexus sp. (gzybioinformatics.cn)
Catalytic1
- It is driven by J-PKAcα, which is a kinase fusion chimera of the J-domain of heat shock co-chaperone DNAJB1 with PKAcα, the catalytic subunit of PKA, which has been used as a model system for the kinase family for the last 40 years. (nih.gov)
Plakophilin1
- 13. Alterations in desmosome size and number coincide with the loss of keratinocyte cohesion in skin with homozygous and heterozygous defects in the desmosomal protein plakophilin 1. (nih.gov)
Kinase domain1
- Characterization of src mutants with host-dependent and dominant-negative phenotypes that define important functional domains outside the protein-tyrosine kinase domain of sre proteins (15, 16, 17, 18). (nih.gov)
Kinases3
- 6. SOcK, MiSTs, MASK and STicKs: the GCKIII (germinal centre kinase III) kinases and their heterologous protein-protein interactions. (nih.gov)
- The long-term goal of our studies is to gain a better understanding of how these large multi-domain kinases affect human health. (nih.gov)
- In conjunction with work in several other labs, these mutants brought the Src-homology (SH) domains 2 and 3 to widespread attention, providing new opportunites for identifying the proteins that are crucial modifiers and targets for Sre-like kinases. (nih.gov)
Subunit1
- Background: Cushing syndrome due to PPNAD is the main endocrine disorder of CNC, an autosomal dominant multiple neoplasia caused by germline inactivating mutations of the subunit type 1A (PRKAR1A) of the protein kinase A (PKA). (endocrine-abstracts.org)
LRRK21
- Despite similar domain organizations, LRRK1 and LRRK2 have distinct interactomes and distinct physiological functions. (nih.gov)
Arabidopsis1
- The demonstration that recombinant Arabidopsis variant P protein has NO-synthesizing activity was a critical piece of evidence leading to the above conclusion. (nih.gov)
Receptors1
- The majority of loss-of function mutations of G protein coupled receptors, leading to diseases, such as diabetes insipidus (V2 vasopressin receptor) or retinitis pigmentosa (rhodopsin) are consecutive to retention of the receptor in the endoplasmic reticulum (ER). (endocrine-abstracts.org)
Function5
- 5. Structure-function analysis of core STRIPAK Proteins: a signaling complex implicated in Golgi polarization. (nih.gov)
- Kinase signaling systems function as multi-domain and multi-component entities to achieve precise regulation of biological processes, and they are frequently deregulated in human diseases. (nih.gov)
- Deletion of DJ-1 in rats affects protein abundance and mitochondrial function at the synapse. (ouhsc.edu)
- These experiments test the function of altered forms of Armadillo that are targeted inside or outside of the nucleus or that contain heterologous transcriptional activator or repressor domains. (nih.gov)
- Biochemical and genetic characterization of Wnt-1 protein as a secretory glycoprotein (11,12) that can function in autocrine or paracrine modes, presumably by interaction with membrane receptor(s). (nih.gov)
Substrates2
- 2. Although many upstream regulators and protein substrates of SFKs have been identified, both the mechanisms of activation and catalysis of SFKs are not fully understood. (edu.au)
- Thus, besides assisting in the identification of potential CHK physiological substrates, our findings shed new light on how CHK recognizes SFKs and other protein substrates. (edu.au)
Genetic1
- Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process. (nih.gov)
Represent2
- Assignment of Homology to Genome Sequences using a Library of Hidden Markov Models that Represent all Proteins of Known Structure. (cam.ac.uk)
- Figure 1 Domain organization of N terminal kinesin, C terminal kinesin and internal kinesin The arrows represent the direction of movement. (chinbullbotany.com)
Complex4
- HN - 2006(1981) BX - Cofilins MH - Actin-Related Protein 2 UI - D051377 MN - D5.750.78.730.246.500 MN - D12.776.220.525.246.500 MS - A PROFILIN binding domain protein that is part of the Arp2-3 complex. (nih.gov)
- HN - 2006(1998) MH - Actin-Related Protein 2-3 Complex UI - D051376 MN - D5.750.78.730.246 MN - D12.776.220.525.246 MS - A complex of seven proteins including ARP2 PROTEIN and ARP3 PROTEIN that plays an essential role in maintenance and assembly of the CYTOSKELETON. (nih.gov)
- We continue to study the impact of J-domain fusion of PKA complex structures and regulation. (nih.gov)
- This paper (Cell 113, 115-125, April 4, 2003) reports results of experiments that together strongly support the conclusion that, in metazoan cells, formation of a complex consisting of the GTP binding protein Ran, the exportin Crm1, and the DNA helicase MCM plays a critical role in limiting DNA replication to a single round each cell cycle. (nih.gov)
Functional1
- We are a basic research laboratory that studies the structural and functional basis of protein kinase signaling. (nih.gov)
Form1
- This paper presents a series of experiments that challenge the conventional view that Armadillo transduces Wingless by combining with Pangolin to form a transcriptional activator. (nih.gov)
Elucidation1
- 1. Elucidation of the inhibitory potential of flavonoids against PKP1 protein in non-small cell lung cancer. (nih.gov)
Phosphorylation1
- This protein, which is highly concentrated around the endoplasmic reticulum, is phosphorylated by v-src, and this phosphorylation reduces the affinity of the protein for smg GDS. (nih.gov)