Nucleocytoplasmic transport molecules that bind to ALPHA KARYOPHERINS in the CYTOSOL and are involved in transport of molecules through the NUCLEAR PORE COMPLEX. Once inside the CELL NUCLEUS beta karyopherins interact with RAN GTP-BINDING PROTEIN and dissociate from alpha karyopherins. Beta karyopherins bound to RAN GTP-BINDING PROTEIN are then re-transported to the cytoplasm where hydrolysis of the GTP of RAN GTP-BINDING PROTEIN causes release of karyopherin beta.
A family of proteins involved in NUCLEOCYTOPLASMIC TRANSPORT. Karyopherins are heteromeric molecules composed two major types of components, ALPHA KARYOPHERINS and BETA KARYOPHERINS, that function together to transport molecules through the NUCLEAR PORE COMPLEX. Several other proteins such as RAN GTP BINDING PROTEIN and CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN bind to karyopherins and participate in the transport process.
Nucleocytoplasmic transport molecules that bind to the NUCLEAR LOCALIZATION SIGNALS of cytoplasmic molecules destined to be imported into the CELL NUCLEUS. Once attached to their cargo they bind to BETA KARYOPHERINS and are transported through the NUCLEAR PORE COMPLEX. Inside the CELL NUCLEUS alpha karyopherins dissociate from beta karypherins and their cargo. They then form a complex with CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN and RAN GTP-BINDING PROTEIN which is exported to the CYTOPLASM.
An opening through the NUCLEAR ENVELOPE formed by the nuclear pore complex which transports nuclear proteins or RNA into or out of the CELL NUCLEUS and which, under some conditions, acts as an ion channel.
Gated transport mechanisms by which proteins or RNA are moved across the NUCLEAR MEMBRANE.
A monomeric GTP-binding protein involved in nucleocytoplasmic transport of proteins into the nucleus and RNA into the cytoplasm. This enzyme was formerly listed as EC 3.6.1.47.
Proteins that form the structure of the NUCLEAR PORE. They are involved in active, facilitated and passive transport of molecules in and out of the CELL NUCLEUS.
Short, predominantly basic amino acid sequences identified as nuclear import signals for some proteins. These sequences are believed to interact with specific receptors at the NUCLEAR PORE.
Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
Intracellular receptors that can be found in the cytoplasm or in the nucleus. They bind to extracellular signaling molecules that migrate through or are transported across the CELL MEMBRANE. Many members of this class of receptors occur in the cytoplasm and are transported to the CELL NUCLEUS upon ligand-binding where they signal via DNA-binding and transcription regulation. Also included in this category are receptors found on INTRACELLULAR MEMBRANES that act via mechanisms similar to CELL SURFACE RECEPTORS.
An interleukin-1 subtype that is synthesized as an inactive membrane-bound pro-protein. Proteolytic processing of the precursor form by CASPASE 1 results in release of the active form of interleukin-1beta from the membrane.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
An 11-kDa protein associated with the outer membrane of many cells including lymphocytes. It is the small subunit of the MHC class I molecule. Association with beta 2-microglobulin is generally required for the transport of class I heavy chains from the endoplasmic reticulum to the cell surface. Beta 2-microglobulin is present in small amounts in serum, csf, and urine of normal people, and to a much greater degree in the urine and plasma of patients with tubular proteinemia, renal failure, or kidney transplants.
One of two major pharmacologically defined classes of adrenergic receptors. The beta adrenergic receptors play an important role in regulating CARDIAC MUSCLE contraction, SMOOTH MUSCLE relaxation, and GLYCOGENOLYSIS.
An integrin beta subunit of approximately 85-kDa in size which has been found in INTEGRIN ALPHAIIB-containing and INTEGRIN ALPHAV-containing heterodimers. Integrin beta3 occurs as three alternatively spliced isoforms, designated beta3A-C.
A factor synthesized in a wide variety of tissues. It acts synergistically with TGF-alpha in inducing phenotypic transformation and can also act as a negative autocrine growth factor. TGF-beta has a potential role in embryonal development, cellular differentiation, hormone secretion, and immune function. TGF-beta is found mostly as homodimer forms of separate gene products TGF-beta1, TGF-beta2 or TGF-beta3. Heterodimers composed of TGF-beta1 and 2 (TGF-beta1.2) or of TGF-beta2 and 3 (TGF-beta2.3) have been isolated. The TGF-beta proteins are synthesized as precursor proteins.
Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.
Body of knowledge related to the use of organisms, cells or cell-derived constituents for the purpose of developing products which are technically, scientifically and clinically useful. Alteration of biologic function at the molecular level (i.e., GENETIC ENGINEERING) is a central focus; laboratory methods used include TRANSFECTION and CLONING technologies, sequence and structure analysis algorithms, computer databases, and gene and protein structure function analysis and prediction.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
A species of nematode that is widely used in biological, biochemical, and genetic studies.
Proteins from the nematode species CAENORHABDITIS ELEGANS. The proteins from this species are the subject of scientific interest in the area of multicellular organism MORPHOGENESIS.
The functional hereditary units of HELMINTHS.
Proteins found in any species of helminth.
A genus of small free-living nematodes. Two species, CAENORHABDITIS ELEGANS and C. briggsae are much used in studies of genetics, development, aging, muscle chemistry, and neuroanatomy.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A casein kinase that was originally described as a monomeric enzyme with a molecular weight of 30-40 kDa. Several ISOENZYMES of casein kinase I have been found which are encoded by separate genes. Many of the casein kinase I isoenzymes have been shown to play distinctive roles in intracellular SIGNAL TRANSDUCTION.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Structures within the nucleus of fungal cells consisting of or containing DNA, which carry genetic information essential to the cell.
Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).
Antibodies produced by a single clone of cells.
The process of moving specific RNA molecules from one cellular compartment or region to another by various sorting and transport mechanisms.
Proteins involved in the process of transporting molecules in and out the cell nucleus. Included here are: NUCLEOPORINS, which are membrane proteins that form the NUCLEAR PORE COMPLEX; KARYOPHERINS, which carry molecules through the nuclear pore complex; and proteins that play a direct role in the transport of karyopherin complexes through the nuclear pore complex.
The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.
Cyclic esters of acylated BUTYRIC ACID containing four carbons in the ring.
A genus of destructive parasitic OOMYCETES in the family Peronosporaceae, order Peronosporales, affecting numerous fruit, vegetable, and other crops. Differentiation of zoospores usually takes place in the sporangium and no vesicle is formed. It was previously considered a fungus.
An annual legume. The SEEDS of this plant are edible and used to produce a variety of SOY FOODS.
Eukaryotes in the group STRAMENOPILES, formerly considered FUNGI, whose exact taxonomic level is unsettled. Many consider Oomycetes (Oomycota) a phylum in the kingdom Stramenopila, or alternatively, as Pseudofungi in the phylum Heterokonta of the kingdom Chromista. They are morphologically similar to fungi but have no close phylogenetic relationship to them. Oomycetes are found in both fresh and salt water as well as in terrestrial environments. (Alexopoulos et al., Introductory Mycology, 4th ed, pp683-4). They produce flagellated, actively motile spores (zoospores) that are pathogenic to many crop plants and FISHES.
Proteins found in any species of algae.
A species of parasitic OOMYCETES in the family Peronosporaceae that is the causative agent of late blight of potato.
Diseases of plants.
Works about randomized clinical trials that compare interventions in clinical settings and which look at a range of effectiveness outcomes and impacts.
Condensation products of aromatic amines and aldehydes forming azomethines substituted on the N atom, containing the general formula R-N:CHR. (From Grant & Hackh's Chemical Dictionary, 5th ed)
A genus of gram-positive, coccoid bacteria consisting of organisms causing variable hemolysis that are normal flora of the intestinal tract. Previously thought to be a member of the genus STREPTOCOCCUS, it is now recognized as a separate genus.
A species of ENTEROVIRUS which is the causal agent of POLIOMYELITIS in humans. Three serotypes (strains) exist. Transmission is by the fecal-oral route, pharyngeal secretions, or mechanical vector (flies). Vaccines with both inactivated and live attenuated virus have proven effective in immunizing against the infection.
A republic in southern Africa east of ZAMBIA and MOZAMBIQUE. Its capital is Lilongwe. It was formerly called Nyasaland.
A greasy substance with a smoky odor and burned taste created by high temperature treatment of BEECH and other WOOD; COAL TAR; or resin of the CREOSOTE BUSH. It contains CRESOLS and POLYCYCLIC AROMATIC HYDROCARBONS which are CARCINOGENS. It has been widely used as wood preservative and in PESTICIDES and had former use medicinally in DISINFECTANTS; LAXATIVES; and DERMATOLOGIC AGENTS.

Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex. (1/444)

Although many viruses replicate in the nucleus, little is known about the processes involved in the nuclear import of viral genomes. We show here that in vitro generated core particles of human hepatitis B virus bind to nuclear pore complexes (NPCs) in digitonin-permeabilized mammalian cells. This only occurred if the cores contained phosphorylated core proteins. Binding was inhibited by wheat germ agglutinin, by antinuclear pore complex antibodies, and by peptides corresponding either to classical nuclear localization signals (NLS) or to COOH-terminal sequences of the core protein. Binding was dependent on the nuclear transport factors importins (karyopherins) alpha and beta. The results suggested that phosphorylation induces exposure of NLS in the COOH-terminal portion of the core protein that allows core binding to the NPCs by the importin- (karyopherin-) mediated pathway. Thus, phosphorylation of the core protein emerged as an important step in the viral replication cycle necessary for transport of the viral genome to the nucleus.  (+info)

Transportin-SR, a nuclear import receptor for SR proteins. (2/444)

The SR proteins, a group of abundant arginine/serine (RS)-rich proteins, are essential pre-mRNA splicing factors that are localized in the nucleus. The RS domain of these proteins serves as a nuclear localization signal. We found that RS domain-bearing proteins do not utilize any of the known nuclear import receptors and identified a novel nuclear import receptor specific for SR proteins. The SR protein import receptor, termed transportin-SR (TRN-SR), binds specifically and directly to the RS domains of ASF/SF2 and SC35 as well as several other SR proteins. The nuclear transport regulator RanGTP abolishes this interaction. Recombinant TRN-SR mediates nuclear import of RS domain- bearing proteins in vitro. TRN-SR has amino acid sequence similarity to several members of the importin beta/transportin family. These findings strongly suggest that TRN-SR is a nuclear import receptor for the SR protein family.  (+info)

GTP hydrolysis links initiation and termination of nuclear import on the nucleoporin nup358. (3/444)

Binding of GTP-bound Ran (RanGTP) to karyopherin beta1 (Kapbeta1) releases import cargo into the nucleus. Using an ultrastructural, biochemical, and functional approach, we have studied the mechanism by which Kapbeta1.RanGTP is recycled at the nuclear pore complex for repeated rounds of import. In vitro, Kapbeta1 bound to the RanBP1-homologous (RBH) domains of Nup358 in the presence of either RanGTP or RanGDP, forming trimeric complexes. The Kapbeta1.RanGTP. RBH complex resisted dissociation by RanBP1 and GTP hydrolysis by Ran GTPase activating protein 1. Ran-dependent binding of gold-conjugated Kapbeta1 to the cytoplasmic fibers of the nuclear pore complex in digitonin-permeabilized cells and RanBP1 competition confirmed the in vitro binding data. Interaction of karyopherin alpha and a classical nuclear localization sequence peptide with the Kapbeta1.RanGTP.RBH complex stimulated GTP hydrolysis by Ran GTPase activating protein 1 both in vitro and in permeabilized cells. This GTP hydrolysis was required for reinitiation of import of a nuclear localization sequence-bearing substrate in permeabilized cells. These data suggest that GTP hydrolysis on the RBH domains of Nup358 couples the termination of one cycle of nuclear import with the initiation of the next.  (+info)

Kap104p-mediated nuclear import. Nuclear localization signals in mRNA-binding proteins and the role of Ran and Rna. (4/444)

Kap104p is a Saccharomyces cerevisiae nuclear import receptor for two essential mRNA-binding proteins, Nab2p and Nab4p/Hrp1p. We demonstrate direct binding of Kap104p to each of these substrates. We have defined the nuclear localization signals in both Nab2p and Nab4p/Hrp1p by Kap104p binding in vitro and KAP104-dependent nuclear import in vivo. The nuclear localization signals map to similar arginine/glycine-rich RNA-binding domains in both proteins and are thus termed rg-nuclear localization signals to distinguish them from classical nuclear localization signals. We also demonstrate that Kap104p, like other known beta-karyopherins (or importins), interacts directly with the small GTPase Ran/Gsp1. However, unlike other known import factors, Ran binding is not sufficient to mediate release of substrates from Kap104p; efficient Ran-GTP-mediated substrate release requires RNA. Also, addition of Kap104p to Nab2p and Nab4p/Hrp1p prebound to single-stranded DNA-cellulose stimulated release of both proteins from the resin. We suggest a simple cycle in which Nab2p and Nab4p/Hrp1p, upon import, are released in the nucleus at sites of transcription by the concerted action of Ran-GTP and binding to newly synthesized mRNA. The resulting ribonucleoprotein complexes are exported to the cytoplasm, where Kap104p rebinds to Nab2p and Nab4p/Hrp1p, contributing to their release from mRNA.  (+info)

The karyopherin Kap122p/Pdr6p imports both subunits of the transcription factor IIA into the nucleus. (5/444)

We discovered a nuclear import pathway mediated by the product of the previously identified Saccharomyces cerevisiae gene PDR6 (pleiotropic drug resistance). This gene product functions as a karyopherin (Kap) for nuclear import. Consistent with previously proposed nomenclature, we have renamed this gene KAP122. Kap122p was localized both to the cytoplasm and the nucleus. As a prominent import substrate of Kap122p, we identified the complex of the large and small subunit (Toa1p and Toa2p, respectively) of the general transcription factor IIA (TFIIA). Recombinant GST-Kap122p formed a complex with recombinant His(6)-Toa1p/Toa2p. In wild-type cells, Toa1p and Toa2p were localized to the nucleus. Consistent with Kap122p being the principal Kap for import of the Toa1p-Toa2p complex, we found that deletion of KAP122 results in increased cytoplasmic localization of both Toa1p and Toa2p. Deletion of KAP122 is not lethal, although deletion of TOA1 and TOA2 is. Together these data suggest that Kap122p is the major Kap for the import of Toa1p-Toa2p into the nucleus. Like other substrate-Kap complexes, the Toa1p/Toa2p/Kap122p complex isolated from yeast cytosol or reconstituted from recombinant proteins, was dissociated by RanGTP but not RanGDP. Kap122p bound to nucleoporins, specifically, to the peptide repeat-containing fragments of Nup1p and Nup2p.  (+info)

The importin/karyopherin Kap114 mediates the nuclear import of TATA-binding protein. (6/444)

Two high copy suppressors of temperature-sensitive TATA-binding protein (TBP) mutants were isolated. One suppressor was TIF51A, which encodes eukaryotic translation initiation factor 5A. The other high copy suppressor, YGL241W, also known as KAP114, is one of 14 importin/karyopherin proteins in yeast. These proteins mediate the transport of specific macromolecules into and out of the nucleus. Cells lacking Kap114 partially mislocalize TBP to the cytoplasm. Kap114 binds TBP in vitro, and binding is disrupted in the presence of GTPgammaS. Therefore, Kap114 is an importer of TBP into the nucleus, but alternative import pathways must also exist.  (+info)

Mlp2p, a component of nuclear pore attached intranuclear filaments, associates with nic96p. (7/444)

A fraction of the yeast nucleoporin Nic96p is localized at the terminal ring of the nuclear basket. When Nic96p was affinity purified from glutaraldehyde-treated spheroplasts, it was found to be associated with Mlp2p. Mlp2p, together with Mlp1p, are the yeast Tpr homologues, which form the nuclear pore-attached intranuclear filaments (Strambio-de-Castillia, C., Blobel, G., and Rout, M. P. (1999) J. Cell Biol. 144, 839-855). Double disruption mutants of MLP1 and MLP2 are viable and apparently not impaired in nucleocytoplasmic transport. However, overproduction of MLP1 causes nuclear accumulation of poly(A)(+) RNA in a chromatin-free area of the nucleus.  (+info)

Purification of protein A-tagged yeast ran reveals association with a novel karyopherin beta family member, Pdr6p. (8/444)

The small GTPase Ran (encoded by GSP1 and GSP2 in yeast) plays a central role in nucleocytoplasmic transport. GSP1 and GSP2 were tagged with protein A and functionally expressed in a gsp1 null mutant. After affinity purification of protein A-tagged Gsp1p or Gsp2p by IgG-Sepharose chromatography, known karyopherin beta transport receptors (e.g. Kap121p and Kap123p) and a novel member of this protein family, Pdr6p, were found to be associated with yeast Ran. Subsequent tagging of Pdr6p with green fluorescent protein revealed association with the nuclear pore complexes in vivo. Thus, functional tagging of yeast Ran allowed the study of its in vivo distribution and interaction with known and novel Ran-binding proteins.  (+info)

beta Karyopherins: Nucleocytoplasmic transport molecules that bind to ALPHA KARYOPHERINS in the CYTOSOL and are involved in transport of molecules through the NUCLEAR PORE COMPLEX. Once inside the CELL NUCLEUS beta karyopherins interact with RAN GTP-BINDING PROTEIN and dissociate from alpha karyopherins. Beta karyopherins bound to RAN GTP-BINDING PROTEIN are then re-transported to the cytoplasm where hydrolysis of the GTP of RAN GTP-BINDING PROTEIN causes release of karyopherin beta.
Transportin-1 (or Importin-β 2) is a protein that in humans is encoded by the TNPO1 gene. This protein is a karyopherin which interacts with nuclear localization sequence to target nuclear proteins to the nucleus. The classical karyopherin receptor complex, such as the complex that uses Importin-β1 (encoded by gene KPNB1), is a heterodimer of an alpha subunit which recognizes the nuclear localization signal and a beta subunit which docks the complex at nucleoporins. However, Transportin-1 can directly bind to the cargo proteins and may not need importin alpha subunit to do it. Transportin-1 is thought to use the same principal mechanism to carry out nuclear transport as other Importins. It mediates docking to the nuclear pore complex through binding to nucleoporin and is subsequently translocated through the pore by an energy requiring mechanism. Then, in the nucleus Ran binds to Transportin-1, it dissociates from cargo, and Transportin-1 is re-exported from the nucleus to the cytoplasm where ...
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This entry represents the N-terminal domain of importin-beta (also known as karyopherins-beta) that is important for the binding of the Ran GTPase protein [(PUBMED:10367892)].. Members of the importin-beta (karyopherin-beta) family can bind and transport cargo by themselves, or can form heterodimers with importin-alpha. As part of a heterodimer, importin-beta mediates interactions with the pore complex, while importin-alpha acts as an adaptor protein to bind the nuclear localisation signal (NLS) on the cargo through the classical NLS import of proteins. Importin-beta is a helicoidal molecule constructed from 19 HEAT repeats. Many nuclear pore proteins contain FG sequence repeats that can bind to HEAT repeats within importins [(PUBMED:12372823), (PUBMED:17161424)], which is important for importin-beta mediated transport.. Ran GTPase helps to control the unidirectional transfer of cargo. The cytoplasm contains primarily RanGDP and the nucleus RanGTP through the actions of RanGAP and RanGEF, ...
View Notes - Lecture 6 10 from BICD 110 at UCSD. Lecture 6 10/10/07 Nuclear Import/Export Nuclear Import Receptors Importins Helps cargo get into nucleus does this by binding to cargo (protein with
Snurportin1 is a novel nuclear import receptor which contains an N-terminal importin beta binding domain which is essential for its function of a snRNP-specific nuclear import receptor [1]. Snurportin1 interacts with m3G-cap where it enhances the m3G-cap dependent nuclear import of U snRNPs in Xenopus laevis oocytes and digitonin-permeabilized HeLa cells [1]. ...
BACKGROUND: Expression of the cellular karyopherin TNPO3/transportin-SR2/Tnp3 is necessary for HIV-1 infection. Depletion of TNPO3 expression in mammalian
BACKGROUND: Expression of the cellular karyopherin TNPO3/transportin-SR2/Tnp3 is necessary for HIV-1 infection. Depletion of TNPO3 expression in mammalian
A late protein is a viral protein that is formed after replication of the virus. One example is VP4 from simian virus 40 (SV40). In Human papillomavirus, two late proteins are involved in capsid formation: a major (L1) and a minor (L2) protein, in the approximate proportion 95:5%. L1 forms a pentameric assembly unit of the viral shell in a manner that closely resembles VP1 from polyomaviruses. Intermolecular disulphide bonding holds the L1 capsid proteins together. L1 capsid proteins can bind via its nuclear localisation signal (NLS) to karyopherins Kapbeta(2) and Kapbeta(3) and inhibit the Kapbeta(2) and Kapbeta(3) nuclear import pathways during the productive phase of the viral life cycle. Surface loops on L1 pentamers contain sites of sequence variation between HPV types. L2 minor capsid proteins enter the nucleus twice during infection: in the initial phase after virion disassembly, and in the productive phase when it assembles into replicated virions along with L1 major capsid proteins. L2 ...
Santa Cruz Biotechnology, Inc. offers a broad range of karyopherin beta 3 CRISPR/Cas9 Knockout plasmids and karyopherin beta 3 Double Nickase Plasmids.
RNA transport from the nucleus to the cytoplasm is fundamental for gene expression. The different RNA species that are produced in the nucleus are exported through the nuclear pore complexes (NPCs) via mobile export receptors. The majority of RNAs, such as tRNAs, rRNAs, and U snRNAs, are transported by specific export receptors, which belong to the karyopherin-beta family proteins. A feature of karyopherins is their regulation by the small GTPase Ran. However, general mRNA export is mechanistically different. Nuclear export of mRNAs is functionally coupled to different steps in gene expression processes, such as transcription, splicing, 3-end formation and even translation ...
RNA transport from the nucleus to the cytoplasm is fundamental for gene expression. The different RNA species that are produced in the nucleus are exported through the nuclear pore complexes (NPCs) via mobile export receptors. The majority of RNAs, such as tRNAs, rRNAs, and U snRNAs, are transported by specific export receptors, which belong to the karyopherin-beta family proteins. A feature of karyopherins is their regulation by the small GTPase Ran. However, general mRNA export is mechanistically different. Nuclear export of mRNAs is functionally coupled to different steps in gene expression processes, such as transcription, splicing, 3-end formation and even translation ...
Doctors noted that a number of researchers studying HIV were interested in separate studies on the same gene, as it plays a certain role in transporting the virus inside cells.. They got in contact with the geneticists in Madrid, who did a lab test and infected the blood taken from the members of the same Spanish family with the virus that causes AIDS.. The experiment gave them a big surprise: the lymphocytes of the patients suffering from that ultra-rare muscular disease were naturally resistant to HIV. The virus couldnt penetrate inside them.. This helps us to understand the transport of the virus in cells much better, explained Jose Alcami, a virologist at the Carlos III Institute of Health in Madrid, who conducts this study. The results were published in the American journal - PLOS Pathogens.. HIV is a well-known virus, the Spanish researcher added, but there are still many things we know less about. For example, we do not know why 5% of infected patients do not develop AIDS. There are ...
KPNB1 (karyopherin (importin) beta 1), Authors: Maria Giubettini, Pauline van der Watt, Annalisa Verrico, Valeria de Turris, Virna Leaner, Patrizia Lavia. Published in: Atlas Genet Cytogenet Oncol Haematol.
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Rabbit Polyclonal Anti-KPNB1 Antibody against Human karyopherin (importin) beta 1. Validated for Immunofluorescence, Immunohistochemistry and Western Blot
In a comparison of the nuclear import of model small and large protein cargos by the importin α/β and transportin pathways, we have made the striking observation that the large cargos require both Ran and hydrolyzable GTP for nuclear import. This contrasts with the import requirements for small cargos that were observed previously and also that were noted in this study: Transportin-mediated import requires neither Ran nor GTP (Englmeier et al., 1999; Ribbeck et al., 1999; Fig. 1), and importin α/β-mediated import requires Ran and a GTP analogue but not GTP hydrolysis (Schwoebel et al., 1998; Fig. 1). We determined that RanGTP is required for the large cargos to traverse the central channel of the NPC, but is not required for association with the cytoplasmic side of the NPC. Furthermore, our data indicate that RanGTP acts to promote large cargo import by directly binding to importin β and transportin, at least in part. These findings are most easily explained by a model in which RanGTP ...
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Goat polyclonal NTF97/Importin beta antibody validated for WB, IHC and tested in Human. Immunogen corresponding to synthetic peptide
Mouse monoclonal NTF97/Importin beta antibody [3E9] validated for WB, IP, Flow Cyt, ChIP, Inhibition, ICC/IF and tested in Human, Mouse and Rat. Referenced in…
Although there appears to be some discrepancy between these new findings and our previous reports that importins are dispensable for the nuclear import of Smads, these observations can be reconciled (Xu et al., 2002, 2003). Our present and previous studies, based on different approaches, may have revealed different nuclear import mechanisms used by basal and activated Smads to enter the nucleus. There are important differences comparing Smads import with or without TGF-β stimulation. Unphosphorylated Smads are monomers, but phosphorylated Smads are assembled into complexes with Smad4 and are thus much larger in size (Wu et al., 2001; Chacko et al., 2004). Moreover, as phospho-Smads accumulate in the nucleus they have to move across the nuclear pore against an ascending concentration gradient of Smads already in the nucleus, whereas unphosphorylated Smads never reach a higher concentration in the nucleus than in the cytoplasm. Thus, importing phospho-Smad complexes and unphosphorylated Smad ...
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Video: Senior author Dr. Michael Fainzilber and lead author Rotem Ben-Tov Perry describe the new Neuron study in a video abstract.. Finding this evidence was far from simple: Importins are so crucial in the cells nucleus that even the smallest embryo could not survive without them. But Rotem Ben-Tov Perry, a research student at the Weizmann Institute who was lead author of the new study, found a way to distinguish the importin beta1 in the cell body from that in the axon: The axonal protein was apparently made from a longer version of messenger RNA, the cells working recipe for building a protein. To see if they could selectively affect just the axonal version of the protein, the Weizmann researchers worked with Drexels Twiss to take advantage of high precision knock-out technology. Rather than knocking a whole gene out of the system, they managed to remove one little piece of the messenger RNAs recipe for manufacturing importins- just the longer bit that sends the RNA to the axon.. Now they ...
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Mega Arginín podporuje nárast hladiny oxidu dusnatého, rozširuje cievy, a tým podporuje zvýšenie odolnosti a vytrvalosti. Tým sa tiež živiny dostávajú rýchlejšie do svalov, oddiaľuje sa únava a posilňuje sa regenerácia svalstva. Arginín môže urýchliť proces hojenia malých svalových zranení a prispieť k nárastu GH. V jednej kapsule poskytuje až 1300 mg arginínu ...
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KASUTUSJUHISED:|br /| Üks kapsel päevas koos iga toiduga, mis sisaldab gluteeni või nii nagu professionaal soovitab. Toidulisandeid ei tohi tarvitada mitmekesise toidusedeli ja tervisliku elustiili asendajana. Ärge ületage päevast annust. Kui olete medit
Gelatina Caps obsahuje hydrolyzovanú želatínu a aktívne aminokyseliny. Chráni kosti, kĺby, spomaľuje opotrebovanie kostí a podporuje rast vlasov a nechtov.
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This is the primary hub for reporting Import Errors on our companion site. Please note that IMPORTS ARE A WORK IN PROGRESS. We are only accepting specif... Tokotna Import Information Error Reports
Molecular modelling and simulation are powerful methods in providing important in-formation on different biological systems to elucidate their structural and functional proper-ties, which cannot be determined in experiment. These methods are applied to analyse versa-tile biological systems: lipid membrane bilayers stabilized by an intercalated single wall carbon nanotube and retroviral proteins such as HIV protease and integrase. HIV-1 integrase has nuclear localization signals (NLS) which play a crucial role in nuclear import of viral preintegration complex (PIC). However, the detailed mechanisms of PIC formation and its nuclear transport are not known. Previously it was shown that NLSs bind to the cell transport machinery e.g. proteins of nuclear pore complex such as transportins. I investigated the interaction of this viral protein HIV-1 integrase with proteins of the nuclear pore complex such as transportin-SR2 (Shityakov et al., 2010). I showed that the transportin-SR2 in nuclear import is ...
Molecular modelling and simulation are powerful methods in providing important in-formation on different biological systems to elucidate their structural and functional proper-ties, which cannot be determined in experiment. These methods are applied to analyse versa-tile biological systems: lipid membrane bilayers stabilized by an intercalated single wall carbon nanotube and retroviral proteins such as HIV protease and integrase. HIV-1 integrase has nuclear localization signals (NLS) which play a crucial role in nuclear import of viral preintegration complex (PIC). However, the detailed mechanisms of PIC formation and its nuclear transport are not known. Previously it was shown that NLSs bind to the cell transport machinery e.g. proteins of nuclear pore complex such as transportins. I investigated the interaction of this viral protein HIV-1 integrase with proteins of the nuclear pore complex such as transportin-SR2 (Shityakov et al., 2010). I showed that the transportin-SR2 in nuclear import is ...
The translocation of macromolecules into the nucleus is a fundamental eukaryotic process, regulating gene expression, cell division and differentiation, but which is impaired in a range of significant diseases including cancer and viral infection. The import of proteins into the nucleus is generally initiated by a specific, high affinity interaction between nuclear localisation signals (NLSs) and nuclear import receptors in the cytoplasm, and terminated through the disassembly of these complexes in the nucleus. For classical NLSs (cNLSs), this import is mediated by the importin-alpha (IMP alpha) adaptor protein, which in turn binds to IMP beta to mediate translocation of nuclear cargo across the nuclear envelope. The interaction and disassembly of import receptor: cargo complexes is reliant on the differential localisation of nucleotide bound Ran across the envelope, maintained in its low affinity, GDP-bound form in the cytoplasm, and its high affinity, GTP-bound form in the nucleus. This in ...
The control of the subcellular localization of cell cycle regulators has emerged as a crucial mechanism in cell division regulation. The active transport of proteins between the nucleus and the cytoplasm is mediated by the transport receptors of the β-karyopherin family. In this work we characterized the terminal phenotype of a mutant strain in β-karyopherin Kap95, a component of the classical nuclear import pathway. When KAP95 was inactivated, most cells arrested at the G2/M phase of the cell cycle, which is in agreement with the results observed in mutants in the other components of this pathway. However, a number of cells accumulate at G1, suggesting a novel role of Kap95 and the classical import pathway at Start. We investigated the localization of Start transcription factors. It is known that Swi6 contains a classical NLS that interacts with importin α. Here we show that the in vivo nuclear import of Swi6 depends on Kap95. For Swi4, we identified a functional NLS between amino acids 371 and 376
Functions in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with the importin-beta subunit KPNB1. Acting autonomously, is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In association with KPNB1 mediates the nuclear import of H1 histone and the Ran
Expression of TNPO3 (IPO12, LGMD1F, MTR10A, TRN-SR, TRN-SR2) in kidney tissue. Antibody staining with HPA039555 in immunohistochemistry.
Expression of TNPO3 (IPO12, LGMD1F, MTR10A, TRN-SR, TRN-SR2) in duodenum tissue. Antibody staining with HPA039555 in immunohistochemistry.
DESCRIPTION (provided by applicant): Karyopherinß proteins mediate nucleocytoplasmic transport through recognition of distinct nuclear localization or export signals (NLSs or NESs). Although there are 19 known Kaps in humans, only three classes of signals for Kap?/Kapß1, Kapß2 (or Transportin) and CRM1, respectively, are known at this time. Most other Kaps recognize diverse sequences that occlude the identity of their signals. This proposal describes structural and biochemical analyses of import systems Kapß2 and Imp5/Kap121 as well as the export-Kap CRM1. Kapß2 mediates nuclear import of RNA binding proteins through their PY-NLSs. Our discovery and understanding of the PY-NLS contributed to the discovery of a defective PY-NLS that causes a subset of amyotrophic lateral sclerosis (ALS). Here, we propose to understand the role of Kapß2 in protein mislocalization and aggregation in ALS. In another aim, we will apply the combined structural, biochemical and bioinformatics approach that we ...
Specialized trafficking systems in eukaryotic cells serve a critical role in partitioning intracellular proteins between the nucleus and cytoplasm. Cytoplasmic proteins (including chromatin remodeling enzymes and transcription factors) must gain access to the nucleus to exert their functions to properly program fundamental cellular events ranging from cell cycle progression to gene transcription. Knowing that nuclear import mediated by members of the karyopherin α family of transport receptors plays a critical role in regulating development and differentiation, we wanted to determine the identity of proteins that are trafficked by this karyopherin α pathway. To this end, we performed a GST pull-down assay using porcine orthologs of karyopherin α1 (KPNA1) and karyopherin α7 (KPNA7) and prey protein derived from porcine fibroblast cells and used a liquid chromatography and tandem mass spectrometry (LC-MS/MS) approach to determine the identity of KPNA1 and KPNA7 interacting proteins. Our screen
Karyopherin (importin) beta 3 RNAi available through Novus Biologicals. Browse our Karyopherin (importin) beta 3 RNAi catalog backed by our Guarantee+.
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importin-alpha-P1, importin alpha 1, IPOA1, karyopherin alpha 2 (RAG cohort 1, importin alpha 1), Karyopherin subunit alpha-2, pendulin, QIP2importin alpha 2, RAG cohort 1, RAG cohort protein 1, RCH1importin subunit alpha-2, SRP1, SRP1alpha, SRP1- ...
In cell-free extracts of eggs that support the assembly of replication-competent nuclei, we discovered that lamin B3 associates with 4 polypeptides (termed SLAPs specifically, soluble lamin associated proteins). using the same dominant-negative mutant, the distribution of additional nucleoporins can be unaffected. Nevertheless, Nup153 recruitment in the nuclear envelope can be lost. Amiloride hydrochloride kinase activity assay Our outcomes indicate that both recruitment and maintenance of Nup153 in the pore are influenced by the integrity of the lamina. oocytes blocks the export of snRNA, mRNA and 5S RNA (Ullman et al., 1999). In addition, Nup153 binds to import cargo, indicating that it is involved directly in nuclear import (Shah et al., 1998). Nup153 has also been reported to shuttle between the nucleoplasmic and cytoplasmic faces of the NPC and this behaviour may be relevant to its function (Nakielny et al., 1999). The nucleoplasmic ring of the NPCs interacts with nuclear lamina filaments ...
Amix Glutamine PepForm Peptides 90 kapsúl Amix™ Glutamine PepForm® Peptides je doplnok stravy obsahujúci unikátnu formu L-Glutamínu vytvoren...
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Popis produktu Originálne indické psyllium (čistota 98%) - prírodná rozpustná vláknina, vhodná pre vegánov. Neobsahuje glutén ani zložky mliečneho či obilného pôvodu.. info_outline Viac info o produkte. ...
Olej z ogórecznika to najbogatsze ródlo od ywcze wa ne Omega-6 kwasów tluszczowych: GLA (kwas gamma-linolenowy). GLA jest prekursorem wielu wa nych prostaglandyn, które sá podobne do hormonów substancje, które mogá mieç wplyw na grubošç, krwi w skórze i stawów, poziom cholesterolu, rozszerzenie i zwé enie naczyñ krwionošnych, zapalenia i wiécej. Od GLA jest rzadko spotykane w ywnošci i wielu czynników bloku zdolnošç organizmu do wlasnych, olej z ogórecznika to niedrogi sposób na poznanie codziennych potrzeb GLA ...
Beta-alanine vytvára vo svaloch karnozín, ktorý zvyšuje silu a vytrvalosť. Zabraňuje svalovej únave, podporuje odbúravanie tukov a nárast svalovej hmoty.
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Sigma-Aldrich offers abstracts and full-text articles by [Ayesha S Don-Salu-Hewage, Siu Yuen Chan, Kathleen M McAndrews, Mahandranauth A Chetram, Michelle R Dawson, Danaya A Bethea, Cimona V Hinton].
KPNA3 antibody, C-term (karyopherin alpha 3 (importin alpha 4)) for ICC/IF, IHC-P, IP, WB. Anti-KPNA3 pAb (GTX26038) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
Plasmid pCMVTNT-T7-KPNA2 from Dr. Bryce Paschals lab contains the insert Karyopherin Alpha 2 and is published in BMC Cell Biol. 2010 . 11():63. This plasmid is available through Addgene.
import getopt import sys import csv from itertools import izip_longest from itertools import izip from memoized import memoized # sudo easy_install mpmath import mpmath #mpmath.mp.dps = 20 # decimal digits of precision @memoized def mpmathcdf(g,df,dps=10): mpmath.mp.dps = dps x,k = mpmath.mpf(g), mpmath.mpf(df) cdf = mpmath.gammainc(k/2, 0, x/2, regularized=True) # floating point precision insufficient, use more precision if cdf == 1.0: if dps > 4000: return cdf # give up after a certain point else: cdf = mpmathcdf(g,df,dps*2) return cdf def GtoP(g,df): assert g >= 0, g return float(1-mpmathcdf(g,df)) import math @memoized def flnf(f): return f*math.log(f) if f>0.5 else 0 @memoized def gtest(a,b,c,d): row1 = a+b row2 = c+d col1 = a+c col2 = b+d total = flnf(a+b+c+d) celltotals = flnf(a)+flnf(b)+flnf(c)+flnf(d) rowtotals = flnf(row1)+flnf(row2) coltotals = flnf(col1)+flnf(col2) # abs is necessary to account for float precision errors when doing the subtraction return abs(2*((celltotals + ...
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IMPORT TUNER (UK) i Tidningsarkivet. Ett digitalt arkiv för svenska tidningar och tidskrifter. Här finns bland annat omslag och innehållstexter för IMPORT TUNER (UK).
Titel: Strategic adaptation to non-reward prediction error qualities and irreducible uncertainty in fMRI Termin: Donnerstag, 18. Januar 2018, 16 Uhr s. t. Ort: Seminarraum des IBB, Malmedyweg 15 (Holzhaus hinter der HNO-Klinik). ...
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"Entrez Gene: KPNB1 karyopherin (importin) beta 1". Köhler M, Speck C, Christiansen M, Bischoff FR, Prehn S, Haller H, Görlich D ... KPNB1 has been shown to interact with: KPNA3, Karyopherin alpha 1, Karyopherin alpha 2, Mothers against decapentaplegic homolog ... a heterodimer of importin alpha and beta subunits. Each of these subunits are part of the karyopherin family of proteins. ... "Ran binding domains promote the interaction of Ran with p97/beta-karyopherin, linking the docking and translocation steps of ...
Shamsher MK, Ploski J, Radu A (2002). "Karyopherin beta 2B participates in mRNA export from the nucleus". Proc. Natl. Acad. Sci ... Ran is involved in the transport of proteins across the nuclear envelope by interacting with karyopherins and changing their ... Kutay U, Izaurralde E, Bischoff FR, Mattaj IW, Görlich D (1997). "Dominant-negative mutants of importin-beta block multiple ... Percipalle P, Clarkson WD, Kent HM, Rhodes D, Stewart M (1997). "Molecular interactions between the importin alpha/beta ...
Shamsher MK, Ploski J, Radu A (October 2002). "Karyopherin beta 2B participates in mRNA export from the nucleus". Proceedings ...
Shamsher MK, Ploski J, Radu A (October 2002). "Karyopherin beta 2B participates in mRNA export from the nucleus". Proceedings ... "Entrez Gene: TNPO2 transportin 2 (importin 3, karyopherin beta 2b)". Fontoura BM, Blobel G, Yaseen NR (October 2000). "The ... "Rules for nuclear localization sequence recognition by karyopherin beta 2". Cell. 126 (3): 543-58. doi:10.1016/j.cell.2006.05. ... nucleoporin Nup98 is a site for GDP/GTP exchange on ran and termination of karyopherin beta 2-mediated nuclear import". The ...
"Rules for nuclear localisation sequence recognition by karyopherin beta 2". Cell. 126 (3): 543-58. doi:10.1016/j.cell.2006.05. ... A protein translated with an NLS will bind strongly to importin (aka karyopherin), and, together, the complex will move through ... also known as transportin or karyopherin β2), which then translocates the cargo protein into the nucleus. The structural basis ... "Crystallographic analysis of the recognition of a nuclear localisation signal by the nuclear import factor karyopherin alpha". ...
Moroianu J, Hijikata M, Blobel G, Radu A (1995). "Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or ... Shamsher MK, Ploski J, Radu A (October 2002). "Karyopherin beta 2B participates in mRNA export from the nucleus". Proc. Natl. ... Nuclear import of hnRNP A1 is mediated by a novel cellular cofactor related to karyopherin-beta. Journal of Cell Science 1997 ... "Nuclear import of hnRNP A1 is mediated by a novel cellular cofactor related to karyopherin-beta". J. Cell Sci. 110 (11): 1325- ...
Zhang C, Sweezey NB, Gagnon S, Muskat B, Koehler D, Post M, Kaplan F (Apr 2000). "A novel karyopherin-beta homolog is ... "Paired-type homeodomain transcription factors are imported into the nucleus by karyopherin 13". Molecular and Cellular Biology ... "Paired-type homeodomain transcription factors are imported into the nucleus by karyopherin 13". Molecular and Cellular Biology ...
For example, the beta-karyopherin superfamily consists of alpha solenoid proteins formed from HEAT repeats; importin beta is a ... Like beta propellers, alpha solenoids are a form of solenoid protein domain commonly found in the proteins comprising the ... A large number of the conserved nucleoporin proteins forming the NPC are either alpha solenoid proteins or consist of a beta ... Most distinctively, a shared domain architecture consisting of an N-terminal beta propeller and a C-terminal alpha solenoid has ...
"The nucleoporin Nup98 is a site for GDP/GTP exchange on ran and termination of karyopherin beta 2-mediated nuclear import". The ... karyopherin alpha3/Qip". The Journal of Biological Chemistry. 275 (14): 10099-104. doi:10.1074/jbc.275.14.10099. PMID 10744690 ...
"The nucleoporin Nup98 is a site for GDP/GTP exchange on ran and termination of karyopherin beta 2-mediated nuclear import". J. ... "The nucleoporin Nup98 is a site for GDP/GTP exchange on ran and termination of karyopherin beta 2-mediated nuclear import". J. ... Bonifaci N, Moroianu J, Radu A, Blobel G (May 1997). "Karyopherin beta2 mediates nuclear import of a mRNA binding protein". ... Yaseen NR, Blobel G (1997). "Cloning and characterization of human karyopherin beta3". Proc. Natl. Acad. Sci. U.S.A. 94 (9): ...
... a heterodimer of importin alpha and beta subunits also known as karyopherins. Importin alpha binds the NLS-containing cargo in ... Interactions between importin beta and the FG repeats of nucleoporins are essential in translocation through the pore complex. ... The protein encoded by this gene is a member of the importin beta family. Structurally, the protein adopts the shape of a right ... September 1997). "Ran-binding protein 5 (RanBP5) is related to the nuclear transport factor importin-beta but interacts ...
... a heterodimer of importin alpha and beta subunits also known as karyopherins. Importin alpha binds the NLS-containing cargo in ... "Entrez Gene: KPNA6 karyopherin alpha 6 (importin alpha 7)". Bukrinsky MI, Haffar OK (2004). "HIV-1 nuclear import: in search of ... Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. The protein encoded by ... Chook YM, Blobel G (2002). "Karyopherins and nuclear import". Curr. Opin. Struct. Biol. 11 (6): 703-15. doi:10.1016/S0959-440X( ...
Moroianu, J; Blobel, G; Radu, A (25 June 1996). "The binding site of karyopherin alpha for karyopherin beta overlaps with a ... "Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import ... Importin alpha, or karyopherin alpha refers to a class of adaptor proteins that are involved in the import of proteins into the ... They are a sub-family of karyopherin proteins. Importin α is known to bind to the nuclear localization signal (NLS) sequence of ...
... karyopherins MeSH D12.776.157.530.750.500.100 - alpha karyopherins MeSH D12.776.157.530.750.500.249 - beta karyopherins MeSH ... gtp-binding protein beta subunits MeSH D12.776.157.325.332.730 - gtp-binding protein gamma subunits MeSH D12.776.157.325. ... large-conductance calcium-activated potassium channel beta subunits MeSH D12.776.157.530.400.600.150.750 - small-conductance ...
... karyopherins MeSH D12.776.543.585.750.500.100 - alpha karyopherins MeSH D12.776.543.585.750.500.249 - beta karyopherins MeSH ... beta-1 MeSH D12.776.543.750.070.300.300.340.725 - receptors, adrenergic, beta-2 MeSH D12.776.543.750.070.300.300.340.900 - ... beta-1 MeSH D12.776.543.750.100.150.300.340.725 - receptors, adrenergic, beta-2 MeSH D12.776.543.750.100.150.300.340.900 - ... beta MeSH D12.776.543.750.720.300.300.300.340.100 - receptors, adrenergic, beta-1 MeSH D12.776.543.750.720.300.300.300.340.200 ...
... moiety to serine or threonince is a common and reversible modification that impairs the protein's binding of karyopherin beta ( ... Bonifaci N, Moroianu J, Radu A, Blobel G (1997). "Karyopherin beta2 mediates nuclear import of an mRNA binding protein". Proc. ...
Importin beta is a of karyopherin that facilitates the transport of cargo proteins into the nucleus. First, it is binding ... Once inside the nucleus, the cargo dissociates from the karyopherins. Importin beta can also carry proteins into the nucleus ... Most proteins require karyopherins to traverse the nuclear pore. Karyopherins can act as importins (i.e. helping proteins get ... Karyopherins at the US National Library of Medicine Medical Subject Headings (MeSH) Illustrations at berkeley.edu Karyopherin ...
Moroianu J, Hijikata M, Blobel G, Radu A (1995). "Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or ... "Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import ... Karyopherin alpha 1 has been shown to interact with KPNB1 and UBR5. GRCh38: Ensembl release 89: ENSG00000114030 - Ensembl, May ... 1996). "Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import". J. Virol. 70 (2): 1027-32. doi: ...
Moroianu J, Hijikata M, Blobel G, Radu A (Jul 1995). "Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 ... "Entrez Gene: KPNA2 karyopherin alpha 2 (RAG cohort 1, importin alpha 1)". Lin CY, Huang PH, Liao WL, Cheng HJ, Huang CF, Kuo JC ... KPNA2 also may play a role in V(D)J recombination Karyopherin alpha 2 has been shown to interact with: ARL4A ITK, KPNB1, PLAG1 ... Braem CV, Kas K, Meyen E, Debiec-Rychter M, Van De Ven WJ, Voz ML (May 2002). "Identification of a karyopherin alpha 2 ...
Another protein, importin (beta) binds to the helical rod section of p62, which also binds NTF2 suggesting the formation of a ... Karyopherin beta2 (transportin), a riboprotein transporter also interacts with p62. P62 also interacts with Nup93, and when ... Yaseen NR, Blobel G (1997). "Cloning and characterization of human karyopherin β3". Proc. Natl. Acad. Sci. U.S.A. 94 (9): 4451- ... Yaseen NR, Blobel G (1997). "Cloning and characterization of human karyopherin β3". Proc. Natl. Acad. Sci. U.S.A. 94 (9): 4451- ...
Representative examples of HEAT repeat proteins include importin β (also known as karyopherin β) family, regulatory subunits of ... The nuclear transport protein importin beta contains 19 HEAT repeats. ... "Structure of importin-beta bound to the IBB domain of importin-alpha". Nature. 399 (6733): 221-229. Bibcode:1999Natur.399..221C ... "Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp". Nature. 399 (6733): 230-237. doi:10.1038/20375. ...
The ARM domain, Armadillo/ beta-catenin-like-repeat, is about a 40 amino acid long tandem repeat that forms superhelix of ... The SRP1 domain is Karyopherin(importin) alpha. This is involved in the exchange of molecules from the nucleus and the ... The ARM domains play a role in mediating the interaction of beta-catenin with its ligand. They are responsible for transduction ... The exchange involves the active transport by a carrier protein called karyopherins. A di-leucine motif is also abundant in ...
... as beta-secretase. Molecular Cellular Neuroscience 14, 419-427 Cite error: The named reference GS was invoked but never defined ... "Crystallographic analysis of the recognition of a nuclear localisation signal by the nuclear import factor karyopherin alpha". ...
... : IPO4, IPO5, IPO7, IPO8, IPO9, IPO11, IPO13 Karyopherin-α: KPNA1, KPNA2, KPNA3, KPNA4, KPNA5, KPNA6 Karyopherin-β: ... "Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking". Cell. 102 (1 ... Importin is a type of karyopherin that transports protein molecules from the cell's cytoplasm to the nucleus. It does so by ... Importin-β is the typical structure of a larger superfamily of karyopherins. The basis of their structure is 18-20 tandem ...
... beta A1 Cyclic nucleotide-gated channel alpha 1 Cyclin A1 Cytochrome P450, family 1, member A1 Defensin, alpha 1 Dystrophin- ... alpha 1 Karyopherin alpha 1 Laminin, alpha 1 Major histocompatibility complex, class II, DP alpha 1 Major histocompatibility ...
Karyopherins will bind to their cargo, and reversibly interact with the FG-repeats in nucleoporins. Karyopherins and their ... There are beta-propeller domain with similarities to WD40 repeats, and more interestingly, unique types of alpha solenoid ( ... In doing so, karyopherins are able to shuttle their cargo across the nuclear envelope. Nucleoporins are only required for the ... Karyopherins can serve as an importin (transporting proteins into the nucleus) or an exportin (transporting proteins out of the ...
It also acts as the docking site of an importing karyopherin. On the cytoplasmic side of the NPC, Nup358 fulfills an analogous ... Ben-Efraim I, Gerace L (2001). "Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear ... Yaseen NR, Blobel G (1997). "Cloning and characterization of human karyopherin beta3". Proc. Natl. Acad. Sci. U.S.A. 94 (9): ... Ben-Efraim, I; Gerace L (January 2001). "Gradient of increasing affinity of importin beta for nucleoporins along the pathway of ...
Braem CV, Kas K, Meyen E, Debiec-Rychter M, Van De Ven WJ, Voz ML (2002). "Identification of a karyopherin alpha 2 recognition ... "Promoter swapping between the genes for a novel zinc finger protein and beta-catenin in pleiomorphic adenomas with t(3;8)(p21; ... PLAG1 has been shown to interact with Karyopherin alpha 2. GRCh38: Ensembl release 89: ENSG00000181690 - Ensembl, May 2017 ... "Identification of a karyopherin alpha 2 recognition site in PLAG1, which functions as a nuclear localization signal". J. Biol. ...
The VP1 protein monomer is primarily composed of beta sheets folded into a jelly roll fold. Interactions between VP1 molecules ... This nuclear import process, mediated by karyopherins, acts on assembled VP1 pentamers in complex with VP2 or VP3; ... within a pentamer involve extensive binding surfaces, mediated in part by interactions between edge beta-strands. The VP1 C- ...
Ben-Efraim I, Gerace L (Jan 2001). "Gradient of increasing affinity of importin beta for nucleoporins along the pathway of ... Bonifaci N, Moroianu J, Radu A, Blobel G (May 1997). "Karyopherin beta2 mediates nuclear import of a mRNA binding protein". ... Ben-Efraim I, Gerace L (Jan 2001). "Gradient of increasing affinity of importin beta for nucleoporins along the pathway of ... Each domain of RanBP2 selectively and directly interacts with distinct proteins such as Ran GTPase, importin-beta, exportin-1/ ...
... beta-mediated nuclear protein import". Cell. 110 (3): 349-60. doi:10.1016/s0092-8674(02)00836-x. PMID 12176322.. ... Karyopherin. References[edit]. *^ a b c GRCh38: Ensembl release 89: ENSG00000082898 - Ensembl, May 2017 ...
The structure of the N-terminal domain of Nup214 reveals a sevenbladed beta-propeller fold followed by a 30-residue C-terminal ... Bonifaci N, Moroianu J, Radu A, Blobel G (May 1997). "Karyopherin beta2 mediates nuclear import of a mRNA binding protein". ... Yaseen NR, Blobel G (Apr 1997). "Cloning and characterization of human karyopherin beta3". Proceedings of the National Academy ... extended peptide segment (CTE). The CTE folds back onto the beta propeller and binds to its bottom face. The structure of the ...
Zuo Y, Qiang L, Farmer SR (March 2006). "Activation of CCAAT/enhancer-binding protein (C/EBP) alpha expression by C/EBP beta ... a member of the karyopherin family, recognizes a two-nucleotide overhang left by the RNase III enzyme Drosha at the 3' end of ...
Takács E, Barabás O, Petoukhov MV, Svergun DI, Vértessy BG (Mar 2009). "Molecular shape and prominent role of beta-strand ... Though both isoforms contain the NLS, the sequence in DUT-M is sequestered away from cognate karyopherins. The isoelectric ... Mol CD, Harris JM, McIntosh EM, Tainer JA (Sep 1996). "Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and ...
... family 1.B.66 Putative beta-barrel porin-2 (BBP2) family 1.B.67 Putative beta barrel porin-4 (BBP4) family 1.B.68 Putative beta ... including karyopherins 1.I.2 Plant plasmodesmata family 2.A.1 Major Facilitator superfamily (MFS), see also Lactose permease, ...
doi:10.1016/S0040-4039(98)00151-8. Murakami, N.; Sugimoto, M.; Kobayashi, M. (2001). "Participation of the beta-hydroxyketone ... can be transported to the cytoplasm by binding to a karyopherin protein called chromosome region maintenance 1 (CRM1)/exportin ...
... this family is further subdivided to the karyopherin-α and the karyopherin-β subfamilies. Other nuclear transport receptors ... proteins.About half of the nucleoporins typically contain solenoid protein domains-either an alpha solenoid or a beta-propeller ... The largest family of nuclear transport receptors are karyopherins, which includes dozens of both importins and exportins; ...
It also interacts directly with the nuclear import receptor Importin-α2 (also known as karyopherin alpha2 or RAG cohort 1), ... "The catenin p120ctn inhibits Kaiso-mediated transcriptional repression of the beta-catenin/TCF target gene matrilysin". ...
Initially described as a transcription factor able to activate expression of the cytokine Interferon beta, IRF-1 was ... "Differential regulation of karyopherin alpha 2 expression by TGF-beta1 and IFN-gamma in normal human epidermal keratinocytes: ... that specifically binds to IFN-beta gene regulatory elements". Cell. 54 (6): 903-13. doi:10.1016/S0092-8674(88)91307-4. PMID ... that specifically binds to IFN-beta gene regulatory elements". Cell. 54 (6): 903-13. doi:10.1016/S0092-8674(88)91307-4. PMID ...
Once inside the CELL NUCLEUS beta karyopherins interact with RAN GTP-BINDING PROTEIN and dissociate from alpha karyopherins. ... Beta karyopherins bound to RAN GTP-BINDING PROTEIN are then re-transported to the cytoplasm where hydrolysis of the GTP of RAN ... GTP-BINDING PROTEIN causes release of karyopherin beta. ... transport molecules that bind to ALPHA KARYOPHERINS in the ... Karyopherin beta; Karyopherin-beta Subunit; beta Importins; p92 nuclear protein; Importin beta; Importins, beta; Karyopherin ...
... beta 3 RNAi available through Novus Biologicals. Browse our Karyopherin (importin) beta 3 RNAi catalog backed by our Guarantee+ ... Karyopherin (importin) beta 3 RNAi. We offer Karyopherin (importin) beta 3 RNAi for use in common research applications. Each ... Alternate Names for Karyopherin (importin) beta 3 RNAi. Karyopherin (importin) beta 3 RNAi, IPO5 RNAi, DKFZp686O1576 RNAi, ... beta 3 RNAi can be used in a variety of model species: Human. Use the list below to choose the Karyopherin (importin) beta 3 ...
... beta 1), Authors: Maria Giubettini, Pauline van der Watt, Annalisa Verrico, Valeria de Turris, Virna Leaner, Patrizia Lavia. ... Human importin beta 1 belongs to the karyopherin beta family of nuclear transport factors, within which 15 evolutionarily ... Biological overview: Importin beta 1 is a prominent member of the karyopherin beta family of transport receptors (reviewed by ... KPNB1 (karyopherin (importin) beta 1). Written. 2013-04. Maria Giubettini, Pauline van der Watt, Annalisa Verrico, Valeria de ...
offers a broad range of karyopherin beta 3 CRISPR/Cas9 Knockout plasmids and karyopherin beta 3 Double Nickase Plasmids. ... karyopherin beta 3 gene silencers are available as karyopherin beta 3 CRISPR/Cas9 Knockout plasmids and karyopherin beta 3 ... karyopherin beta 3 Antibodies for analysis of cellular responses to karyopherin beta 3 CRISPR Products ... karyopherin beta 3 CRISPR Knockout, HDR and Nickase Knockout Plasmids PRODUCT NAME. CATALOG #. Species. APPLICATIONS. MARKER. ...
... or karyopherins, also known as importins/exportins) that bind and … ... beta Karyopherins / metabolism* Substances * NUP2 protein, S cerevisiae * Nuclear Pore Complex Proteins ... The dynamics of karyopherin-mediated nuclear transport Biochem Cell Biol. 2001;79(5):603-12. ... Biochemical characterization of individual karyopherins has led to the identification of many of their cargoes and to the ...
Karyopherin Subunit Beta 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The ... KPNB1 (Karyopherin Subunit Beta 1) is a Protein Coding gene. Among its related pathways are Regulation of cholesterol ... At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta ... At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta ...
Recombinant Human karyopherin Beta 1 RECOMBINANT & NATURAL PROTEINS \ pro-1001 for more molecular products just contact us ... Recombinant Human karyopherin Beta 1 RECOMBINANT & NATURAL PROTEINS. Related products : Recombinant Human karyopherin Beta 1 ... WP1045: TGF-beta Receptor Signaling Pathway. WP1048: TGF Beta Signaling Pathway. WP105: Fatty Acid Beta Oxidation 2. WP1058: ... WP113: TGF Beta Signaling Pathway. WP1161: TGF-beta Receptor Signaling Pathway. WP1164: TGF Beta Signaling Pathway. WP1177: ...
beta Karyopherins Grant support * U01 CA086322/CA/NCI NIH HHS/United States ...
KAP95; Karyopherin (importin) beta [Intracellular trafficking and secretion]. sd00044. Location:388 → 416. HEAT; HEAT repeat [ ... KAP95; Karyopherin (importin) beta [Intracellular trafficking and secretion]. sd00044. Location:388 → 416. HEAT; HEAT repeat [ ... Evolutionary and transcriptional analysis of karyopherin beta superfamily proteins. Quan Y, et al. Mol Cell Proteomics, 2008 ...
beta Karyopherins. *Signal Transduction. *Virus Replication. *EZH2. *Up-Regulation. *Enhancer of Zeste Homolog 2 Protein ...
Karyopherin subunit beta-4Curated. Karyopherin-1231 Publication. ,p>Manually curated information that is based on statements in ... Importin subunit beta-4Add BLAST. 1113. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical view ... "Kap104p: a karyopherin involved in the nuclear transport of messenger RNA binding proteins.". Aitchison J.D., Blobel G., Rout M ... "Kap104p: a karyopherin involved in the nuclear transport of messenger RNA binding proteins.". Aitchison J.D., Blobel G., Rout M ...
Karyopherin beta 4; SWI4; Swi4p: transcription factor; USS1; Uss1p: core protein of small nuclear ribonucleoprotein; YER113C; ...
KAP95; Karyopherin (importin) beta [Intracellular trafficking and secretion]. sd00044. Location:330 → 353. HEAT; HEAT repeat [ ... Data indicate a mechanism of epidermal growth factor receptor (EGFR) regulation through the importin beta family member RAN- ...
Characterization of p92, Karyopherin .BETA., Co-Purified with N-Acetylglucosamine-Bearing Nucleoporins from Rat Liver Nuclear ... Characterization of p92, Karyopherin β, Co-Purified with N-Acetylglucosamine-Bearing Nucleoporins from Rat Liver Nuclear ...
"Entrez Gene: KPNB1 karyopherin (importin) beta 1". Köhler M, Speck C, Christiansen M, Bischoff FR, Prehn S, Haller H, Görlich D ... KPNB1 has been shown to interact with: KPNA3, Karyopherin alpha 1, Karyopherin alpha 2, Mothers against decapentaplegic homolog ... a heterodimer of importin alpha and beta subunits. Each of these subunits are part of the karyopherin family of proteins. ... "Ran binding domains promote the interaction of Ran with p97/beta-karyopherin, linking the docking and translocation steps of ...
Mouse monoclonal NTF97/Importin beta antibody [3E9] validated for WB, IP, Flow Cyt, ChIP, Inhibition, ICC/IF and tested in ... The first step, docking at the nuclear pore complex, requires a 54/56 kDa nuclear localization signal receptor (a-karyopherin, ... At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta ... Anti-NTF97/Importin beta antibody [3E9]. See all NTF97/Importin beta primary antibodies. ...
Karyopherin beta 2B participates in mRNA export from the nucleus. (PMID: 12384575) Shamsher MK … Radu A (Proceedings of the ... Belongs to the importin beta family. Importin beta-2 subfamily.. Family:. * Belongs to the importin beta family. Importin beta- ... Transportin 2 (Importin 3, Karyopherin Beta 2b) 3 * Karyopherin Beta 2b, Transportin 3 ...
... which belong to the karyopherin-beta family proteins. A feature of karyopherins is their regulation by the small GTPase Ran. ...
Importin beta is a of karyopherin that facilitates the transport of cargo proteins into the nucleus. First, it is binding ... Once inside the nucleus, the cargo dissociates from the karyopherins. Importin beta can also carry proteins into the nucleus ... Most proteins require karyopherins to traverse the nuclear pore. Karyopherins can act as importins (i.e. helping proteins get ... Karyopherins at the US National Library of Medicine Medical Subject Headings (MeSH) Illustrations at berkeley.edu Karyopherin ...
transportin 2 (importin 3, karyopherin beta 2b). MGI:2384849 Go Annotations as Summary Text (Tabular View) (GO Graph). ...
Xu, D., Farmer, A., and Chook, Y. M. (2010). Recognition of nuclear targeting signals by Karyopherin-beta proteins. Curr. Opin ... Beaulieu, J. M., Sotnikova, T. D., Marion, S., Lefkowitz, R. J., Gainetdinov, R. R., and Caron, M. G. (2005). An Akt/beta- ... For example, it has been shown that DARPP-32 binds directly to the splicing factor transformer 2-beta 1 (tra2-beta1) and ... Wang, B., Li, Z., Xu, L., Goggi, J., Yu, Y., and Zhou, J. (2004). Molecular cloning and characterization of rat karyopherin ...
... we show that these necleoporins can be isolated from yeast extracts by affinity chromatography on karyopherin Kap95p-coated ... we show that these necleoporins can be isolated from yeast extracts by affinity chromatography on karyopherin Kap95p-coated ...
karyopherin beta. protein-coding. KAP104. Kap104p. protein-coding. KTR7. putative mannosyltransferase. protein-coding. ... beta-glucan synthesis-associated protein KRE6. protein-coding. KSP1. putative serine/threonine protein kinase KSP1. protein- ...
beta Karyopherins/genetics*. Minor. *Base Sequence. *Blotting, Western. *Exome/genetics. *Female. *Fluorescent Antibody ...
Soniat, M., and Chook, Y. M. (2015). Nuclear localization signals for four distinct karyopherin-beta nuclear import systems. ... The PY-NLS is recognized for nuclear import by karyopherin-β2 (Kapβ2) in humans and by its ortholog Kap104 in yeast (Lee et al ... The results suggest that the P. sojae karyopherins that presumably bind to these NLSs do so more weakly than in other ... Chook, Y. M., and Suel, K. E. (2011). Nuclear import by karyopherin-βs: recognition and inhibition. Biochim. Biophys. Acta 1813 ...
YNL189W SRP1; karyopherin alpha YLR347C KAP95; karyopherin beta YJR042W NUP85; Nup85p YMR047C NUP116; FG-nucleoporin NUP116 ... YMR307W GAS1; 1,3-beta-glucanosyltransferase GAS1 YLR343W GAS2; 1,3-beta-glucanosyltransferase YMR215W GAS3; putative 1,3-beta- ... YDR238C SEC26; coatomer subunit beta YGL137W SEC27; coatomer subunit beta YLR262C YPT6; Rab family GTPase YPT6 YHR129C ARP1; ... YOL132W GAS4; 1,3-beta-glucanosyltransferase YOL030W GAS5; 1,3-beta-glucanosyltransferase YFR031C SMC2; condensin subunit SMC2 ...
karyopherin subunit beta 1. protein-coding. KRTAP3-3. keratin associated protein 3-3. protein-coding. ... potassium calcium-activated channel subfamily M regulatory beta subunit 2. protein-coding. ... potassium calcium-activated channel subfamily M regulatory beta subunit 4. protein-coding. ...
transportin 2 (importin 3, karyopherin beta 2b) Gene [Source:MGI Symbol;Acc:MGI:2384849]. ...
"Remodeling of the pioneer translation initiation complex involves translation and the karyopherin importin beta." Genes & ... "A beta zero-thalassemic beta-globin RNA that is labile in bone marrow cells is relatively stable in HeLa cells." Nucleic acids ... "Novel metabolism of several beta zero-thalassemic beta-globin mRNAs in the erythroid tissues of transgenic mice." The EMBO ... "Unstable beta-globin mRNA in mRNA-deficient beta o thalassemia." Cell.. 1981 Dec 0; 27(3 Pt 2):543-53. ...
  • Once inside the CELL NUCLEUS beta karyopherins interact with RAN GTP-BINDING PROTEIN and dissociate from alpha karyopherins. (curehunter.com)
  • Beta karyopherins bound to RAN GTP-BINDING PROTEIN are then re-transported to the cytoplasm where hydrolysis of the GTP of RAN GTP-BINDING PROTEIN causes release of karyopherin beta. (curehunter.com)
  • The human importin beta 1 protein is composed of 876 aminoacidic residues, with a molecular weight of 97 kDa (Görlich et al. (atlasgeneticsoncology.org)
  • Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. (genecards.org)
  • The protein encoded by this gene is a member of the importin beta family. (genecards.org)
  • KPNB1 (Karyopherin Subunit Beta 1) is a Protein Coding gene. (genecards.org)
  • Data indicate a mechanism of epidermal growth factor receptor (EGFR) regulation through the importin beta family member RAN-binding protein 6 (RanBP6). (nih.gov)
  • Full length native protein (purified) corresponding to Cow NTF97/Importin beta. (abcam.com)
  • Importin subunit beta-1 is a protein that in humans is encoded by the KPNB1 gene. (wikipedia.org)
  • 2000) Purification of protein Atagged yeast ran reveals association with a novel karyopherin beta family member, Pdr6p. (springer.com)
  • This topology has been found with a number of repeats and domains, including the armadillo repeat (found in beta-catenins and importins), the HEAT repeat (found in protein phosphatase 2a and initiation factor eIF4G), the PHAT domain (found in Smaug RNA-binding protein), the leucine-rich repeat variant, the Pumilo repeat, and in the H regulatory subunit of V-type ATPases. (embl.de)
  • As part of a heterodimer, importin-beta mediates interactions with the pore complex, while importin-alpha acts as an adaptor protein to bind the nuclear localisation signal (NLS) on the cargo through the classical NLS import of proteins. (embl.de)
  • Karyopherin α2 was first identified as Rch-1, an NLS receptor which interacts with the RAG-1 recombination-activating protein in developing B and T cells. (bdbiosciences.com)
  • Parmi ces facteurs de l'hôte, l'étude de karyopherin subunit beta 1 (KPNB1) et de heat shock protein 60 (HSP60) a été priorisée. (umontreal.ca)
  • Karyopherin, a cytosolic, heterodimeric protein complex consisting of alpha and beta subunits, is responsible for targeting proteins with nuclear localization signals to the nuclear pore complex. (acris-antibodies.com)
  • Phosphorylation of the capsid is thought to induce exposure of nuclear localization signal in the C-terminal portion of the capsid protein that allows binding to the nuclear pore complex via the importin (karyopherin-) alpha and beta. (uniprot.org)
  • Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes. (semanticscholar.org)
  • The recognition of SMAD s by TGF-beta receptor type I may be facilitated by auxiliary protein Zinc finger FYVE domain containing 9 ( SARA ) [ 2 ]. (bio-rad.com)
  • FK506 binding protein 1A 12kDa ( FKBP12 ) inhibits TGF-beta signaling by binding to the unphosphorylated GS regions of TGF-beta receptor type I . This interaction locks the kinase catalytic center of the TGF-beta receptor type I in an unproductive conformation [ 2 ], [ 4 ]. (bio-rad.com)
  • Nuclear transport receptors are an integral part of the transport system and belong predominantly to the karyopherin protein superfamily [ 5 ]. (oncotarget.com)
  • Moroianu J, Blobel G, Radu A. Nuclear protein import: Ran-GTP dissociates the karyopherin alphabeta heterodimer by displacing alpha from an overlapping binding site on beta. (proteopedia.org)
  • Ste20 forms protein complexes with two β-karyopherins, Kap121 (Kpn β3) and Kap123 (Kpn β1-like karyopherin). (scitechnol.com)
  • Structured summary of protein interactions: Karyopherin alpha-1 physically interacts with WDR42A by anti tag co-immunoprecipitation (View interaction) WDR42A physically interacts with Karyopherin alpha-1 by pull down (View interaction) Karyopherin beta-1 physically interacts with WDR42A by anti tag co-immunoprecipitation (View interaction) WDR42A physically interacts with CRM1 by anti tag co-immunoprecipitation (View interaction) WDR42A and RAN colocalize by fluorescence microscopy (View interaction). (houstonmethodist.org)
  • A gene on chromosome 3q21 that encodes an alpha subunit of karyopherin, which plays a key role in nuclear protein import as an adapter protein for nuclear receptor KPNB1. (thefreedictionary.com)
  • Importin Beta antibody LS-C287366 is an unconjugated rabbit polyclonal antibody to Importin Beta (KPNB1) from human, mouse, rat and other species. (lsbio.com)
  • The regulated exchange of proteins and nucleic acids between the nucleus and cytoplasm demands a complex interplay between nuclear pore complexes (NPCs), which provide conduits in the nuclear envelope, and mobile transport receptors (or karyopherins, also known as importins/exportins) that bind and mediate the translocation of cargoes through the NPCs. (nih.gov)
  • Karyopherins (kaps, also known as importins/exportins) bind to specific import or export signals and mediate substrate docking to the NPC. (rupress.org)
  • Active transport of large molecules through these pore complexes require carrier proteins, called karyopherins (importins and exportins), which shuttle between the two compartments. (embl.de)
  • At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. (genecards.org)
  • After their synthesis, TFs are transported into the nucleus a process regulated by karyopherins commonly known as importin alpha and β. (plantphysiol.org)
  • We have shown that 20S core particles are translocated into the nucleus as inactive precursor complexes via the classical karyopherin alpha/beta import pathway (Lehmann et al. (hu-berlin.de)
  • This gene encodes the beta subunit of the karyopherin receptor complex which interacts with nuclear localization signals to target nuclear proteins to the nucleus. (creativebiomart.net)
  • Cytosolic proteins bearing a classical nuclear localization signal enter the nucleus bound to a heterodimer of importin-alpha and importin-beta (also called karyopherin-alpha and -beta). (rcsb.org)
  • In the nucleus, RanGTP binds to importin-beta within the importin/cargo complex, causing a conformational change in importin-beta that releases it from importin-alpha-bound cargo. (embl.de)
  • SMAD3 translocation to the nucleus depends on binding of Importin (karyopherin)-beta [ 5 ]. (bio-rad.com)
  • Karyopherins, including alpha and beta types, are transport proteins in the eukaryotic cell that carry cargoes across nuclear pore complexes into or out of the nucleus. (readbyqxmd.com)
  • Although OGFr pharmacologically resembles classical opioid receptors (recognizes opioids, naloxone (Nal) reversibility, stereospecificity), it shares no sequence homology, has a different cellular localization (detected in the outer nuclear envelope, nucleus, and perinuclear cytoplasm [6,16-19]), and undergoes trafficking into the nucleus in a process that requires nuclear localization signals and transport by karyopherin b and Ran [17,20]. (scirp.org)
  • Phosphorylated IRF-5 is transported to the nucleus by binding to nuclear import proteins karyopherin-alpha1 and -beta1. (bvsalud.org)
  • Lane 1: 1:2500, lane 2: 1:5000, lane 3: 1:10,000 dilution of the mouse anti-karyopherin antibody. (bdbiosciences.com)
  • karyopherin beta 3 gene silencers are available as karyopherin beta 3 CRISPR/Cas9 Knockout plasmids and karyopherin beta 3 Double Nickase Plasmids. (scbt.com)
  • karyopherin beta 3 CRISPR/dCas9 Activation Plasmids and CRISPR Lenti Activation Systems for gene activation are also available. (scbt.com)
  • TGF-beta induces transcription of the human SMAD7 gene through activation of SMAD3 [ 12 ], and transcription factor Ets variant gene 1 ( ER81 ) [ 13 ]. (bio-rad.com)
  • KPNA6 - Karyopherin alpha 6 (importin alpha 7), also known as KPNA6, is a human gene. (enacademic.com)
  • KPNA4 - Karyopherin alpha 4 (importin alpha 3), also known as KPNA4, is a human gene. (enacademic.com)
  • The import of proteins containing a nuclear localization signal (NLS) requires the NLS import receptor, a heterodimer of importin alpha and beta subunits also known as karyopherins. (genecards.org)
  • The karyopherin receptor complex is a heterodimer of an alpha subunit which recognizes the nuclear localization signal and a beta subunit which docks the complex at nucleoporins. (creativebiomart.net)
  • The structure indicates that significant conformational changes occur when importin-beta binds or releases the IBB domain domain and suggests how dissociation of the importin-alpha/beta heterodimer may be achieved upon nuclear entry. (rcsb.org)
  • There are two subfamilies of karyopherins: importin alpha and importin beta ( Tamura and Hara-Nishimura, 2014 ). (plantphysiol.org)
  • Binds to a beta-like import receptor binding (BIB) domain of RPL23A. (genecards.org)
  • The first step, docking at the nuclear pore complex, requires a 54/56 kDa nuclear localization signal receptor (a-karyopherin, importin-a, SRP-a) and the nuclear transport factor p97 (NTF 97, b-karyopherin, importin-b). (abcam.com)
  • SRP1 (nucleoprotein interactor 1, NPI 1) is the alpha subunit of karyopherin, which acts as the receptor for the targeted protein's nuclear localization signal (Moroianu J. Crit 1997). (acris-antibodies.com)
  • TGF-beta 1 initiates signaling by binding to and bringing together type I and type II receptor serine/threonine kinases ( TGF-beta receptor type I and II ) on the cell surface. (bio-rad.com)
  • This allows TGF-beta receptor type II to phosphorylate the TGF-beta receptor type I kinase domain. (bio-rad.com)
  • TGF-beta receptor type I then propagates the signal through phosphorylation of the SMAD family member ( SMAD ) proteins [ 2 ], [ 3 ]. (bio-rad.com)
  • SMAD7 inhibits TGF-beta receptor type I [ 3 ] via competition with SMAD3 or SMAD2 for binding. (bio-rad.com)
  • Each of these subunits are part of the karyopherin family of proteins. (wikipedia.org)
  • The N-terminal fragment of adaptin alpha-C and beta subunits. (embl.de)
  • The karyopherin dimer dissociates during import, a process mediated by RanGTP, which binds to karyopherin ß and promotes the release of both subunits from the docking site (Moroianu J. Crit 1997). (acris-antibodies.com)
  • The six alpha subunits form a central wheel in the assembly, and the beta subunits form domes on the top and bottom of the wheel, creating six reaction chambers within which each ACP can reach the six active sites through surprisingly modest movements. (theologyonline.com)
  • an extended C-terminal region of importin beta 1 contains sites of interaction with members of the importin alpha subfamily transport receptors (Importin alpha-binding domain, IAB), through which importin beta 1 interacts indirectly with import cargoes (Percipalle et al. (atlasgeneticsoncology.org)
  • The majority of RNAs, such as tRNAs, rRNAs, and U snRNAs, are transported by specific export receptors, which belong to the karyopherin-beta family proteins. (genome.jp)
  • Nucleocytoplasmic transport molecules that bind to ALPHA KARYOPHERINS in the CYTOSOL and are involved in transport of molecules through the NUCLEAR PORE COMPLEX. (curehunter.com)
  • Interestingly, the arginine-rich NLS of Rex uses importin beta for import but does so by a mechanism that is importin alpha independent. (curehunter.com)
  • Importin alpha binds the NLS-containing cargo in the cytoplasm and importin beta docks the complex at the cytoplasmic side of the nuclear pore complex. (genecards.org)
  • Für 20S Proteasomen konnten Lehmann und Mitarbeitende (2002, JMB, 317, 401) zeigen, dass Vorläuferkomplexe über den Karyopherin alpha/beta abhängigen Importweg in den Zellkern gelangen und dort zu 20S Proteasomen heranreifen. (hu-berlin.de)
  • In dieser Arbeit wird gezeigt, dass die nukleäre Lokalisation der 19S Regulatorkomplexe ebenfalls von Karyopherin alpha/beta abhängt. (hu-berlin.de)
  • Unsere Daten unterstützen ein Modell wonach die nukleären 26S Proteasomen aus Subkomplexen zusammengelagert werden, die durch Karyopherin alpha/beta in den Zellkern gelangen. (hu-berlin.de)
  • Here, we provide evidence that nuclear import of base and lid complexes also depends on karyopherin alpha/beta. (hu-berlin.de)
  • Our data support the model by which nuclear 26S proteasomes are assembled from subcomplexes imported by karyopherin alpha/beta. (hu-berlin.de)
  • Here we report the crystal structure of human importin-beta bound to the IBB domain of importin-alpha, determined at 2.5 A and 2.3 A resolution in two crystal forms. (rcsb.org)
  • Members of the importin-alpha (karyopherin-alpha) family can form heterodimers with importin-beta. (embl.de)
  • the alpha subunit binds the substrate and the beta subunit acts as an adaptor (Moroianu J, et al. (acris-antibodies.com)
  • Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal and beta subunit interacts with peptide repeat-containing nucleoporins. (semanticscholar.org)
  • In this study, full open reading frames of one beta and three alpha types of karyopherin were cloned from cDNA of the domestic silkworm (Bombyx mori). (readbyqxmd.com)
  • Evolutionary and transcriptional analysis of karyopherin beta superfamily proteins. (nih.gov)
  • Ran is involved in the transport of proteins across the nuclear envelope by interacting with karyopherins and changing their ability to bind or release cargo molecules. (wikipedia.org)
  • The mutagenized Ste20 PAK from S. cerevisiae was tested for its ability to bind to karyopherins. (scitechnol.com)
  • Behrens, Functional interaction of beta-catenin with the transcription factor LEF-1. (xenbase.org)
  • En utilisant les fondements de cette étude, un essai à haut débit dans les cellules vivantes a été réalisé pour identifier de nouveaux composés anti-VHC ciblant une nouvelle interaction NS3/4A-NS3/4A. (umontreal.ca)
  • at mitotic onset nucleo-cytoplasmic transport ceases and importin beta 1 assumes new functions as an inhibitor of mitotic factors with which it interacts and participating in many mitotic steps (see below). (atlasgeneticsoncology.org)
  • Interactions between importin beta and the FG repeats of nucleoporins are essential in translocation through the pore complex. (genecards.org)
  • Many cargoes destined for nuclear import carry nuclear localization signals that are recognized by karyopherins (Kaps). (rupress.org)
  • Karyopherin beta, mediates nuclear import of ribosomal proteins prior to assembly into ribosomes and. (yeastrc.org)
  • Heterodimers belonging to a highly conserved family of proteins called karyopherins are required for successful nuclear localization of cytosolic proteins. (bdbiosciences.com)
  • TSC22 domain family member 1 ( TSC-22 ) as a SMAD4 -interacting positively regulates TGF-beta -dependent erythroid cell differentiation [ 11 ]. (bio-rad.com)
  • Belongs to the importin beta family. (abcam.cn)
  • Biochemical characterization of individual karyopherins has led to the identification of many of their cargoes and to the elucidation of the mechanisms by which they mediate transport. (nih.gov)
  • Characterization of p92, Karyopherin .BETA. (nii.ac.jp)
  • GENTAUR suppliers human normal cells, cell lines, RNA extracts and lots of antibodies and ELISA kits to Human proteins as well as Recombinant Human karyopherin Beta 1 RECOMBINANT & NATURAL PROTEINS. (antibody-antibodies.com)
  • Almeida, Wnt proteins prevent apoptosis of both uncommitted osteoblast progenitors and differentiated osteoblasts by beta-catenin-dependent and -independent signaling cascades involving Src/ERK and phosphatidylinositol 3-kinase/AKT. (xenbase.org)
  • The PAK I binding to karyopherins is separable from its kinase function. (scitechnol.com)
  • Pubmed ID: 11909949 To further our understanding of how the nucleocytoplasmic transport machinery interfaces with its cargoes and how this affects cellular physiology, we investigated the molecular mechanisms of phenotypes associated with mutations in karyopherin Kap121p. (jove.com)
  • The mutant-expression phenotypes were examined to establish the β -karyopherin deficiency. (scitechnol.com)
  • This domain is structurally similar to armadillo and Heat repeats of beta-catenin and karyopherin-beta, respectively. (rcsb.org)
  • The alphas all had one importin-beta-binding (IBB) domain, and eight, four, or seven armadillo/beta-catenin-like repeats. (readbyqxmd.com)
  • V-ski sarcoma viral oncogene homolog ( Ski ) and SKI-like oncogene ( SnoN ) modulate the nuclear activity of SMAD and function as corepressors antagonize TGF-beta signaling [ 4 ], [ 8 ]. (bio-rad.com)
  • Kpn β1 (karyopherin subunit β1) is a nuclear-transport factor that increases cell proliferation and cancer growth [ 1 - 4 ]. (scitechnol.com)
  • Here, we show that these necleoporins can be isolated from yeast extracts by affinity chromatography on karyopherin Kap95p-coated beads. (nih.gov)
  • This domain is found close to the N terminus of yeast exportin 1 (Xpo1, Crm1, P14068 ), as well as adjacent to the N-terminal domain of importin-beta ( IPR001494 ). (ebi.ac.uk)