alpha Karyopherins: 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.Karyopherins: 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.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.Nuclear Pore: 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.Active Transport, Cell Nucleus: Gated transport mechanisms by which proteins or RNA are moved across the NUCLEAR MEMBRANE.ran GTP-Binding Protein: 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.Nuclear Pore Complex Proteins: 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.Nuclear Localization Signals: 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.Cell Nucleus: 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)Saccharomyces cerevisiae Proteins: 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.Nuclear Proteins: 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.Saccharomyces cerevisiae: 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.Receptors, Cytoplasmic and Nuclear: 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.Protein Binding: 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.alpha 1-Antitrypsin: Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.Receptors, Adrenergic, alpha: One of the two major pharmacological subdivisions of adrenergic receptors that were originally defined by the relative potencies of various adrenergic compounds. The alpha receptors were initially described as excitatory receptors that post-junctionally stimulate SMOOTH MUSCLE contraction. However, further analysis has revealed a more complex picture involving several alpha receptor subtypes and their involvement in feedback regulation.Hypoxia-Inducible Factor 1, alpha Subunit: Hypoxia-inducible factor 1, alpha subunit is a basic helix-loop-helix transcription factor that is regulated by OXYGEN availability and is targeted for degradation by VHL TUMOR SUPPRESSOR PROTEIN.alpha7 Nicotinic Acetylcholine Receptor: A member of the NICOTINIC ACETYLCHOLINE RECEPTOR subfamily of the LIGAND-GATED ION CHANNEL family. It consists entirely of pentameric a7 subunits expressed in the CNS, autonomic nervous system, vascular system, lymphocytes and spleen.Integrin alpha3beta1: Cell surface receptor for LAMININ, epiligrin, FIBRONECTINS, entactin, and COLLAGEN. Integrin alpha3beta1 is the major integrin present in EPITHELIAL CELLS, where it plays a role in the assembly of BASEMENT MEMBRANE as well as in cell migration, and may regulate the functions of other integrins. Two alternatively spliced isoforms of the alpha subunit (INTEGRIN ALPHA3), are differentially expressed in different cell types.Integrin alpha4: An integrin alpha subunit that is unique in that it does not contain an I domain, and its proteolytic cleavage site is near the middle of the extracellular portion of the polypeptide rather than close to the membrane as in other integrin alpha subunits.Integrin alpha6: An integrin alpha subunit that primarily associates with INTEGRIN BETA1 or INTEGRIN BETA4 to form laminin-binding heterodimers. Integrin alpha6 has two alternatively spliced isoforms: integrin alpha6A and integrin alpha6B, which differ in their cytoplasmic domains and are regulated in a tissue-specific and developmental stage-specific manner.Integrin alpha5beta1: An integrin found in FIBROBLASTS; PLATELETS; MONOCYTES, and LYMPHOCYTES. Integrin alpha5beta1 is the classical receptor for FIBRONECTIN, but it also functions as a receptor for LAMININ and several other EXTRACELLULAR MATRIX PROTEINS.Integrin alpha4beta1: Integrin alpha4beta1 is a FIBRONECTIN and VCAM-1 receptor present on LYMPHOCYTES; MONOCYTES; EOSINOPHILS; NK CELLS and thymocytes. It is involved in both cell-cell and cell- EXTRACELLULAR MATRIX adhesion and plays a role in INFLAMMATION, hematopoietic cell homing and immune function, and has been implicated in skeletal MYOGENESIS; NEURAL CREST migration and proliferation, lymphocyte maturation and morphogenesis of the PLACENTA and HEART.Interleukin-1alpha: An interleukin-1 subtype that occurs as a membrane-bound pro-protein form that is cleaved by proteases to form a secreted mature form. Unlike INTERLEUKIN-1BETA both membrane-bound and secreted forms of interleukin-1alpha are biologically active.Integrin alpha2beta1: An integrin found on fibroblasts, platelets, endothelial and epithelial cells, and lymphocytes where it functions as a receptor for COLLAGEN and LAMININ. Although originally referred to as the collagen receptor, it is one of several receptors for collagen. Ligand binding to integrin alpha2beta1 triggers a cascade of intracellular signaling, including activation of p38 MAP kinase.Receptors, Adrenergic, alpha-1: A subclass of alpha-adrenergic receptors that mediate contraction of SMOOTH MUSCLE in a variety of tissues such as ARTERIOLES; VEINS; and the UTERUS. They are usually found on postsynaptic membranes and signal through GQ-G11 G-PROTEINS.Integrin alpha5: This integrin alpha subunit combines with INTEGRIN BETA1 to form a receptor (INTEGRIN ALPHA5BETA1) that binds FIBRONECTIN and LAMININ. It undergoes posttranslational cleavage into a heavy and a light chain that are connected by disulfide bonds.Integrin alpha1beta1: Integrin alpha1beta1 functions as a receptor for LAMININ and COLLAGEN. It is widely expressed during development, but in the adult is the predominant laminin receptor (RECEPTORS, LAMININ) in mature SMOOTH MUSCLE CELLS, where it is important for maintenance of the differentiated phenotype of these cells. Integrin alpha1beta1 is also found in LYMPHOCYTES and microvascular endothelial cells, and may play a role in angiogenesis. In SCHWANN CELLS and neural crest cells, it is involved in cell migration. Integrin alpha1beta1 is also known as VLA-1 and CD49a-CD29.Authorship: The profession of writing. Also the identity of the writer as the creator of a literary production.Knowledge Bases: Collections of facts, assumptions, beliefs, and heuristics that are used in combination with databases to achieve desired results, such as a diagnosis, an interpretation, or a solution to a problem (From McGraw Hill Dictionary of Scientific and Technical Terms, 6th ed).Nucleoplasmins: A family of histone molecular chaperones that play roles in sperm CHROMATIN decondensation and CHROMATIN ASSEMBLY in fertilized eggs. They were originally discovered in XENOPUS egg extracts as histone-binding factors that mediate nucleosome formation in vitro.Dictionaries, MedicalDictionaries as Topic: Lists of words, usually in alphabetical order, giving information about form, pronunciation, etymology, grammar, and meaning.Rats, Inbred BUFGTP-Binding 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.-.Graft Survival: The survival of a graft in a host, the factors responsible for the survival and the changes occurring within the graft during growth in the host.Kidney Transplantation: The transference of a kidney from one human or animal to another.Delayed Graft Function: General dysfunction of an organ occurring immediately following its transplantation. The term most frequently refers to renal dysfunction following KIDNEY TRANSPLANTATION.Graft Rejection: An immune response with both cellular and humoral components, directed against an allogeneic transplant, whose tissue antigens are not compatible with those of the recipient.Risk Factors: An aspect of personal behavior or lifestyle, environmental exposure, or inborn or inherited characteristic, which, on the basis of epidemiologic evidence, is known to be associated with a health-related condition considered important to prevent.Algorithms: A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task.Antibodies: 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).Antibody Specificity: The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Antibodies, Viral: Immunoglobulins produced in response to VIRAL ANTIGENS.Antibodies, Bacterial: Immunoglobulins produced in a response to BACTERIAL ANTIGENS.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Carcinoma, Non-Small-Cell Lung: A heterogeneous aggregate of at least three distinct histological types of lung cancer, including SQUAMOUS CELL CARCINOMA; ADENOCARCINOMA; and LARGE CELL CARCINOMA. They are dealt with collectively because of their shared treatment strategy.Lung Neoplasms: Tumors or cancer of the LUNG.Gene Dosage: The number of copies of a given gene present in the cell of an organism. An increase in gene dosage (by GENE DUPLICATION for example) can result in higher levels of gene product formation. GENE DOSAGE COMPENSATION mechanisms result in adjustments to the level GENE EXPRESSION when there are changes or differences in gene dosage.Genomic Instability: An increased tendency of the GENOME to acquire MUTATIONS when various processes involved in maintaining and replicating the genome are dysfunctional.Gene Expression Profiling: The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Neoplasm Staging: Methods which attempt to express in replicable terms the extent of the neoplasm in the patient.

Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex. (1/392)

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)

Deciphering the nuclear import pathway for the cytoskeletal red cell protein 4.1R. (2/392)

The erythroid membrane cytoskeletal protein 4.1 is the prototypical member of a genetically and topologically complex family that is generated by combinatorial alternative splicing pathways and is localized at diverse intracellular sites including the nucleus. To explore the molecular determinants for nuclear localization, we transfected COS-7 cells with epitope-tagged versions of natural red cell protein 4.1 (4.1R) isoforms as well as mutagenized and truncated derivatives. Two distant topological sorting signals were required for efficient nuclear import of the 4.1R80 isoform: a basic peptide, KKKRER, encoded by alternative exon 16 and acting as a weak core nuclear localization signal (4.1R NLS), and an acidic peptide, EED, encoded by alternative exon 5. 4.1R80 isoforms lacking either of these two exons showed decreased nuclear import. Fusion of various 4.1R80 constructs to the cytoplasmic reporter protein pyruvate kinase confirmed a requirement for both motifs for full NLS function. 4.1R80 was efficiently imported in the nuclei of digitonin-permeabilized COS-7 cells in the presence of recombinant Rch1 (human importin alpha2), importin beta, and GTPase Ran. Quantitative analysis of protein-protein interactions using a resonant mirror detection technique showed that 4.1R80 bound to Rch1 in vitro with high affinity (KD = 30 nM). The affinity decreased at least 7- and 20-fold, respectively, if the EED motif in exon 5 or if 4.1R NLS in exon 16 was lacking or mutated, confirming that both motifs were required for efficient importin-mediated nuclear import of 4.1R80.  (+info)

Nuclear import of plasmid DNA in digitonin-permeabilized cells requires both cytoplasmic factors and specific DNA sequences. (3/392)

Although much is known about the mechanisms of signal-mediated protein and RNA nuclear import and export, little is understood concerning the nuclear import of plasmid DNA. Plasmids between 4.2 and 14.4 kilobases were specifically labeled using a fluorescein-conjugated peptide nucleic acid clamp. The resulting substrates were capable of gene expression and nuclear localization in microinjected cells in the absence of cell division. To elucidate the requirements for plasmid nuclear import, a digitonin-permeabilized cell system was adapted to follow the nuclear localization of plasmids. Nuclear import of labeled plasmid was time- and energy-dependent, was inhibited by the lectin wheat germ agglutinin, and showed an absolute requirement for cytoplasmic extract. Addition of nuclear extract alone did not support plasmid nuclear import but in combination with cytoplasm stimulated plasmid nuclear localization. Whereas addition of purified importin alpha, importin beta, and RAN was sufficient to support protein nuclear import, plasmid nuclear import also required the addition of nuclear extract. Finally, nuclear import of plasmid DNA was sequence-specific, requiring a region of the SV40 early promoter and enhancer. Taken together, these results confirm and extend our findings in microinjected cells and support a protein-mediated mechanism for plasmid nuclear import.  (+info)

Nuclear import of RPA in Xenopus egg extracts requires a novel protein XRIPalpha but not importin alpha. (4/392)

Replication protein A (RPA) is a eukaryotic single-stranded (ss) DNA-binding protein that is essential for general DNA metabolism. RPA consists of three subunits (70, 33 and 14 kDa). We have identified by two-hybrid screening a novel Xenopus protein called XRIPalpha that interacts with the ssDNA-binding domain of the largest subunit of RPA. XRIPalpha homologues are found in human and in Drosophila but not in yeast. XRIPalpha is complexed with RPA in Xenopus egg extracts together with another 90 kDa protein that was identified as importin beta. We have demonstrated that XRIPalpha, but not importin alpha, is required for nuclear import of RPA. Immunodepletion of XRIPalpha from the egg extracts blocks nuclear import of RPA but not that of nucleoplasmin, a classical import substrate. RPA import can be restored by addition of recombinant XRIPalpha. Conversely, depletion of importin alpha blocks import of nucleoplasmin but not that of RPA. GST-XRIPalpha pull-down assay shows that XRIPalpha interacts directly with recombinant importin beta as well as with RPA in vitro. Finally, RPA import can be reconstituted from the recombinant proteins. We propose that XRIPalpha plays the role of importin alpha in the RPA import scheme: XRIPalpha serves as an adaptor to link RPA to importin beta.  (+info)

The direction of transport through the nuclear pore can be inverted. (5/392)

Transport of macromolecules across the nuclear envelope is an active process that depends on soluble factors including the GTPase Ran. Ran-GTP is predominantly located in the nucleus and has been shown to regulate cargo binding and release of import and export receptors in their respective target compartments. Recently, it was shown that transport of receptor-cargo complexes across the nuclear pore complex (NPC) does not depend on GTP-hydrolysis by Ran; however, the mechanism of translocation is still poorly understood. Here, we show that the direction of transport through the NPC can be inverted in the presence of high concentrations of cytoplasmic Ran-GTP. Under these conditions, two different classes of export cargoes are transported into the nucleus in the absence of GTP hydrolysis. The inverted transport is very rapid and can be blocked by known inhibitors of nuclear protein export. These results suggest that the NPC functions as a facilitated transport channel, allowing the selective translocation of receptor-cargo complexes. We conclude that the directionality of nucleocytoplasmic transport is determined mainly by the compartmentalized distribution of Ran-GTP.  (+info)

Cellular uptake and nuclear delivery of recombinant adenovirus penton base. (6/392)

An Ad2 capsid component, the penton base, expressed as recombinant protein, was found to be capable of affecting the entire entry pathway of adenovirion in HeLa cells, i.e., cell attachment, endocytosis, vesicular escape, intracytoplasmic movement, and translocation through the nuclear pore complex. Data with pentamerization-defective mutants suggested that none of these successive steps depended upon penton base pentamer status, indicating that the peptide domains responsible for these functions were carried by the monomer. Observations performed with wild-type (WT) and an integrin-binding-site double-mutant (K288E340) suggested that the penton base could enter the cell via an alternative, RGD- and LDV-independent, pathway. Of three mutants that were found to be defective in nuclear addressing in insect cells, only one, W165H, was also altered in nuclear transport in HeLa cells. The other two, W119H and RRR547EQQ, showed a WT pattern of nuclear localization in HeLa cells, suggesting that the region including tryptophan-119 and the basic signal at position 547 did not act as a nuclear localization signal in the human cell context. The integrity of cellular structures and the cytoskeleton seemed to be required for the vectorial movement and nuclear import of WT penton base, as suggested by experiments using permeabilized HeLa cells, isolated nuclear membranes, and cytoskeleton-targeted drugs.  (+info)

The yeast nucleoporin Nup2p is involved in nuclear export of importin alpha/Srp1p. (7/392)

The importin alpha.beta heterodimer mediates nuclear import of proteins containing classical nuclear localization signals. After carrying its cargo into the nucleus, the importin dimer dissociates, and Srp1p (the yeast importin alpha subunit) is recycled to the cytoplasm in a complex with Cse1p and RanGTP. Nup2p is a yeast FXFG nucleoporin that contains a Ran-binding domain. We find that export of Srp1p from the nucleus is impaired in Deltanup2 mutants. Also, Srp1p fusion proteins accumulate at the nuclear rim in wild-type cells but accumulate in the nuclear interior in Deltanup2 cells. A deletion of NUP2 shows genetic interactions with mutants in SRP1 and PRP20, which encodes the Ran nucleotide exchange factor. Srp1p binds directly to an N-terminal domain of Nup2p. This region of Nup2p is sufficient to allow accumulation of an Srp1p fusion protein at the nuclear rim, but the C-terminal Ran-binding domain of Nup2p is required for efficient Srp1p export. Formation of the Srp1p.Cse1p. RanGTP export complex releases Srp1p from its binding site in Nup2p. We propose that Nup2p may act as a scaffold that facilitates formation of the Srp1p export complex.  (+info)

A bipartite nuclear localization signal is required for p53 nuclear import regulated by a carboxyl-terminal domain. (8/392)

Abnormal p53 cellular localization has been considered to be one of the mechanisms that could inactivate p53 function. To understand the regulation of p53 cellular trafficking, we have previously identified two p53 domains involved in its localization. A basic domain, Lys(305)-Arg(306), is required for p53 nuclear import, and a carboxyl-terminal domain, namely the cytoplasmic sequestration domain (CSD) from residues 326-355, could block the nuclear import of Lys(305) or Arg(306) mutated p53. To characterize further the function of these two domains, we demonstrate in this report that the previously described major nuclear localization signal works together with Lys(305)-Arg(306) to form a bipartite and functional nuclear localization sequence (NLS) for p53 nuclear import. The CSD could block the binding of p53 to the NLS receptor, importin alpha, and reduce the efficiency of p53 nuclear import in MCF-7, H1299, and Saos-2 cells. The blocking effect of the CSD is not due to the enhancement of nuclear export or oligomerization of the p53. These results indicate that the CSD can regulate p53 nuclear import by controlling access of the NLS to importin alpha binding.  (+info)

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 ...
1.I.1 The Eukaryotic Nuclear Pore Complex (E-NPC) Family [formerly 1.A.75]. Numerous NPC proteins, called nucleoporins, have been identified and characterized from vertebrates and yeast (Brohawn et al., 2009). Thirty such proteins are recognized constituents of the yeast NPC, and at least 50 nucleopore proteins have been characterized from vertebrates. Many of these proteins have been tabulated for (1) S. cerevisiae and (2) vertebrates by Stoffler et al. (1999) and Tran and Wente (2006). How they function in transport is poorly defined. It is known, however, that nuclear proteins contain short sequences called nuclear localization sequences (NLS) that target them for nuclear import. A nuclear localization sequence receptor and several cytosolic factors appear to play roles in nuclear import of NLS-bearing proteins. Nuclear export signals (NESs) have also been identified. Several different forms of each type of targeting signal have been identified that lack homology to each other and may be ...
KPNA4 (karyopherin alpha 4), also known as importin alpha 3, is a member of the importin alpha family of proteins which includes KPNA1 (importin alpha…
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
Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoproteins nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoproteins
Proteins that carry a nuclear localization signal (NLS) are transported into the nucleus by the importin-alpha/beta heterodimer. Importin-alpha binds the NLS, while importin-beta mediates translocation through the nuclear pore complex. After translocation, RanGTP binds importin-beta and displaces importin-alpha. Importin-alpha must then be returned to the cytoplasm, leaving the NLS protein behind. The protein encoded by this gene binds strongly to NLS-free importin-alpha, and this binding is released in the cytoplasm by the combined action of RANBP1 and RANGAP1. In addition, the encoded protein may play a role both in apoptosis and in cell proliferation. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jan 2012 ...
Importin alpha 5/KPNA1/SRP1 products available through Novus Biologicals. Browse our Importin alpha 5/KPNA1/SRP1 product catalog backed by our Guarantee+.
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- ...
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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
The importin-alpha/beta complex and the GTPase Ran mediate nuclear import of proteins with a classical nuclear localization sigl. The protein encoded…
Karyopherin (importin) beta 3 RNAi available through Novus Biologicals. Browse our Karyopherin (importin) beta 3 RNAi catalog backed by our Guarantee+.
Hey-mutant mouse hearts at embryonic day E14.5 were shown to react to the knock out of Hey2 with several up-regualted genes. This up-regulation is due to the lack of Hey2 and cannot be explained by the structural changes in heart morphology as shown using control animals. Part of the gene regulation was further validated using in situ hybridization. Hey1 was located to the nucleus in immunofluorescence experiments. However, experiments on protein level showed also amount of Hey1 within the cytoplasm. The nuclear localization of Hey1 was unchanged during all cell cycle phases as well as when CaMKII was co-expressed or other cellular pathways were inhibited or stimulated. Hey1 does not seem to interact with the nuclear transport proteins importin-alpha and -beta, therefore it still needs to be elucidated how Hey1 is transported into the nucleus ...
A nuclear receptor likely involved in nuclear protein import is described. Purified ATP-depleted yeast nuclei show saturable high-affinity binding of the yeast nuclear protein Mcm1. The dissociation constant for the binding is 0.5 microM, and the number of binding sites is approximately 3,500 per nucleus, equivalent to 10-30 binding sites per nuclear pore. Mcm1 competes with other yeast nuclear proteins Ste12 and Swi5, but not with Rap1 or Nop1, indicating that there may be different types of import receptors. Bound Mcm1 is resistant to extraction by nucleases, salt, and non-ionic detergent, but can be released by 5 M urea, suggesting that Mcm1 binds to a yeast equivalent of the nuclear pore complex-lamina fraction of higher eukaryotes ...
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.
I am currently working on a computer user interface for specifying (not designing) mutational protein libraries. In addition to a online forms interface I would like to be able to directly import protein sequence data and multiple sequence alignments from a file. I was wondering whether any researchers would like to comment on what types of programs and data formats are popular. In paticular, I am considering an function to directly import Excel spreadsheet files (ala GoCore, etc.). Any comments would be greatly appreciated. Rick Colman UC Irvine ...
Gene Information The signal sequence receptor (SSR) is a glycosylated endoplasmic reticulum (ER) membrane receptor associated with protein translocation across the ER membrane. The SSR is comprised of four membrane proteins/subunits: alpha beta gamma and delta. The first two are glycosylated subunits and the latter two are non-glycosylated subunits. This gene encodes the gamma subunit which is predicted to span the membrane four times. [provided by RefSeq Aug 2010]. ...
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Looking for online definition of karyopherin alpha 5 in the Medical Dictionary? karyopherin alpha 5 explanation free. What is karyopherin alpha 5? Meaning of karyopherin alpha 5 medical term. What does karyopherin alpha 5 mean?
Satellite cells are stem cells with an essential role in skeletal muscle repair. Precise regulation of gene expression is critical for proper satellite cell quiescence, proliferation, differentiation and self-renewal. Nuclear proteins required for gene expression are dependent on the nucleocytoplasmic transport machinery to access to nucleus, however little is known about regulation of nuclear transport in satellite cells. The best characterized nuclear import pathway is classical nuclear import which depends on a classical nuclear localization signal (cNLS) in a cargo protein and the heterodimeric import receptors, karyopherin alpha (KPNA) and beta (KPNB). Multiple KPNA1 paralogs exist and can differ in importing specific cNLS proteins required for cell differentiation and function. We show that transcripts for six Kpna paralogs underwent distinct changes in mouse satellite cells during muscle regeneration accompanied by changes in cNLS proteins in nuclei. Depletion of KPNA1, the most ...
Importin is a type of karyopherin that transports protein molecules into the nucleus by binding to specific recognition sequences, called nuclear localization sequences (NLS). Importin has two subunits, importin α and importin β. Members of the importin-β family can bind and transport cargo by themselves, or can form heterodimers with importin-α. As part of a heterodimer, importin-β mediates interactions with the pore complex, while importin-α acts as an adaptor protein to bind the nuclear localisation signal (NLS) on the cargo. The NLS-Importin α-Importin β trimer dissociates after binding to Ran GTP inside the nucleus, with the two importin proteins being recycled to the cytoplasm for further use. Importin can exist as either a heterodimer of importin-α/β or as a monomer of Importin-β. Importin-α was first isolated in 1994 by a group including Enno Hartmann, based at the Max Delbrück Center for Molecular Medicine. The process of nuclear protein import had already been ...
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
Our results define a bipartite NLS that is integrated within the DNA-recognition region of IRF3. We mapped the NLS of IRF3 to aa 64-130, partially overlapping with the DBD. Basic amino acids KR77/78 and RK86/87 are required for efficient nuclear import of IRF3. Significantly, we demonstrate that the NLS of IRF3 also plays an important role in the DNA-binding activity.. The IRF family contains nine mammalian members (IRF1, IRF2, IRF3, IRF4, IRF5, IRF6, IRF7, IRF8, and IRF9), which are most conserved in their DBD. IRF1 and IRF2, which are closely related to each other, contain a conserved NLS located immediately C-terminal to the DBD, involving aa 120-138 (33). IRF4, IRF8, and IRF9 are highly conserved with each other and use the homologous NLS (aa 66-85) to direct their accumulation in the nucleus (34). Interestingly, IRF5 contains two monopartite consensus NLSs, a N-terminal NLS and a C-terminal NLS (35). Our study, together with previous reports, demonstrated that the NLSs of IRFs are generally ...
We have characterized the nuclear localization signal (NLS) of XRCC1 structurally using X-ray crystallography and functionally using fluorescence imaging. Crystallography and binding studies confirm the bipartite nature of the XRCC1 NLS interaction with Importin α (Impα) in which the major and minor binding motifs are separated by ,20 residues, and resolve previous inconsistent determinations. Binding studies of peptides corresponding to the bipartite NLS, as well as its major and minor binding motifs, to both wild-type and mutated forms of Impα reveal pronounced cooperative binding behavior that is generated by the proximity effect of the tethered major and minor motifs of the NLS. The cooperativity stems from the increased local concentration of the second motif near its cognate binding site that is a consequence of the stepwise binding behavior of the bipartite NLS. We predict that the stepwise dissociation of the NLS from Impα facilitates unloading by providing a partially complexed ...
Export receptor for importin-alpha. Mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates (cargos) have been released into the nucleoplasm. In the nucleus binds cooperatively to importin-alpha and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the importin-alpha from the export receptor. CSE1L/XPO2 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus ...
Das 26S Proteasom führt die letzen Schritte des essentiellen, Ubiquitin abhängigen Proteinabbaus durch, indem es ubiquitinierte und fehlgefaltete Proteine erkennt und eliminiert. Da es in S. cerevisiae während allen Stadien der Zellteilung vornehmlich im Zellkern lokalisiert ist, ist der Importweg dieses 2,5 MDa umfassenden proteolytischen Komplexes in den Zellkern von besonderem Interesse. Das 26S Proteasom unterteilt sich in das katalytisch aktive 20S Proteasom sowie den 19S Regulatorkomplex. 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. In dieser Arbeit wird gezeigt, dass die nukleäre Lokalisation der 19S Regulatorkomplexe ebenfalls von Karyopherin alpha/beta abhängt. Die Untersuchung der potentiellen klassischen Kernlokalisationssequenzen (cNLS) in den Untereinheiten des 19S Base Subkomplex ergab, dass ...
Santa Cruz Biotechnology, Inc. offers a broad range of karyopherin beta 3 CRISPR/Cas9 Knockout plasmids and karyopherin beta 3 Double Nickase Plasmids.
... , Authors: Maria Giubettini, Pauline van der Watt, Annalisa Verrico, Valeria de Turris, Virna Leaner, Patrizia Lavia. Published in: Atlas Genet Cytogenet Oncol Haematol.
1EE5: Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha.
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]. ...
Baycrest is pleased to share our Quality Improvement Plan (QIP) with our clients, family members and broader community. The QIP is a requirement under the Excellent Care For All Act, 2010 and was approved by the Baycrest Board of Directors.. This plan describes the key actions we are committed to taking to make improvements to the care and services you receive. As in previous years, these improvement priorities are rooted in our strategic goal to deliver exceptional quality of care and quality of life for our patients and residents.. Our QIP was developed with extensive feedback from clients, staff and physicians and reflects what they told us matters most to deliver safe, high quality care. Along with a review of our improvement achievements and challenges over the past year, required standards, legislation, and best practices, our QIP reflects consistent themes across our organization while at the same time, making sure these priorities reflect the specific needs of our long term care ...
Importin and nucleoplasmin complex, molecular model. Nucleoplasmin tags proteins for entry to the cell nucleus, while importin transports the protein across the nuclear membrane. - Stock Image C025/1566
is a type of protein that moves other protein molecules into the nucleus by binding to a specific recognition sequence, called the nuclear localization signal (NLS). Importin is classified as a karyopherin.…
Yanxiao Gong, Shengli Zhang, Ping Xu, Zhenda Xie and Shining Zhu. Realization of a hybrid squeeze operator via a single chi(2) nonlinear photonic crystal and its applications in quantum information ...
4BA3: Crystal Structure of Rice Importin-Alpha and Structural Basis of its Interaction with Plant-Specific Nuclear Localization Signals.
Buy our Recombinant Human KPNA2 protein. Ab123205 is a full length protein produced in Escherichia coli and has been validated in SDS-PAGE. Abcam provides free…
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.
Predicted to have nuclear import signal receptor activity and nuclear localization sequence binding activity. Involved in negative regulation of muscle cell differentiation and protein import into nucleus. Predicted to localize to the cytoplasm and nucleus. Orthologous to human TNPO2 (transportin 2 ...
The Genetics Society of America (GSA), founded in 1931, is the professional membership organization for scientific researchers and educators in the field of genetics. Our members work to advance knowledge in the basic mechanisms of inheritance, from the molecular to the population level.. Online ISSN: 1943-2631. ...
Hand Therapy Group has been recognised for the quality and safety of their service with the award of accreditation by Quality Innovation Performance (QIP) at our Macquarie, Pacific and Hills Norwest practices. QIP is Australias most comprehensive not-for-profit accreditation organisation, dedicated to delivering accreditation and support services to a diverse…. ...
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 ...
I am looking for NLS for lac-Z gene. I believe the NLS is now available commercially, but I have looked up some common suppliers with no success. I would appreciate if anyone can help me out with this. Or if knows of any source where I can get hold of NLS-LacZ plasmid. Thanks Obaid Khan ...
313175.1 Except import which takes way too long. I took a full export of WE8ISO8859p1 Database and now importing it in AL32UTF8. It is always difficult to prove where the slowness is coming from; but I think it has to do something with NLS_LENGTH_SEMANTICS. On the same server; if new database was in WE8ISO8859P1, a 5 million row table import took 2 hours; but in Al32UTF8 with NLS_LENGTH_SEMANTICS it is taking 1 day!!! Any idea how to improve the performance of import. ...
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
Correct targeting of nuclear proteins is mediated by nuclear localization sequences (NLS) which permit specific binding to the nucleus and subsequent translocation across the nuclear envelope via the nuclear pore complex. It is proposed that nuclear import is facilitated by NLS-receptors which reside in the cytoplasm and at the nuclear pore. These NLS-receptors could facilitate an early step of nuclear protein import, i.e. targeting and binding of nuclear proteins at the nuclear pore. We have generated anti-idiotype antibodies against the SV40 T-antigen nuclear localization sequence that allowed us to study NLS-binding proteins in a variety of different organisms. Proteins of similar size are recognized by these antibodies in yeast, Drosophila, rat and human cells. Cytological analysis indicates that the NLS-binding proteins reside in part at nuclear pores. One of the proteins recognized by anti-idiotype antibodies is identical to a previously identified NLS-binding protein. Using isolated yeast ...
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, ...
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 ...
The SRP1 domain is Karyopherin(importin) alpha. This is involved in the exchange of molecules from the nucleus and the ... The SRP1 domain encodes alpha-Karyopherin (importin) and is known for intracellular trafficking and secretion on the membrane. ... The exchange involves the active transport by a carrier protein called karyopherins. A di-leucine motif is also abundant in ...
"Entrez Gene: KPNA3 karyopherin alpha 3 (importin alpha 4)". Köhler, M; Speck C; Christiansen M; Bischoff F R; Prehn S; Haller H ... The similarities among these proteins suggests that karyopherin alpha-3 may be involved in the nuclear transport system. KPNA3 ... "Isolation and mapping of karyopherin alpha 3 (KPNA3), a human gene that is highly homologous to genes encoding Xenopus importin ... Importin subunit alpha-3 is a protein that in humans is encoded by the KPNA3 gene. The transport of molecules between the ...
"Entrez Gene: KPNA6 karyopherin alpha 6 (importin alpha 7)". Bukrinsky MI, Haffar OK (2004). "HIV-1 nuclear import: in search of ... a heterodimer of importin alpha and beta subunits also known as karyopherins. Importin alpha binds the NLS-containing cargo in ... Importin subunit alpha-7 is a protein that in humans is encoded by the KPNA6 gene. Nucleocytoplasmic transport, a signal- and ... Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. The protein encoded by ...
"Entrez Gene: KPNA4 karyopherin alpha 4 (importin alpha 3)". Liu L, McBride KM, Reich NC (Jun 2005). "STAT3 nuclear import is ... "Cloning of two novel human importin-alpha subunits and analysis of the expression pattern of the importin-alpha protein family ... Importin subunit alpha-4 is a protein that in humans is encoded by the KPNA4 gene. The nuclear import of karyophilic proteins ... Gallay P, Stitt V, Mundy C, Oettinger M, Trono D (Feb 1996). "Role of the karyopherin pathway in human immunodeficiency virus ...
"Entrez Gene: KPNA5 karyopherin alpha 5 (importin alpha 6)". Bukrinsky MI, Haffar OK (2004). "HIV-1 nuclear import: in search of ... "Cloning of two novel human importin-alpha subunits and analysis of the expression pattern of the importin-alpha protein family ... Importin subunit alpha-6 is a protein that in humans is encoded by the KPNA5 gene. The transport of molecules between the ... 1996). "Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import". J. Virol. 70 (2): 1027-32. PMC ...
... has been shown to interact with Karyopherin alpha 2. GRCh38: Ensembl release 89: ENSG00000122644 - Ensembl, May 2017 ...
Braem CV, Kas K, Meyen E, Debiec-Rychter M, Van De Ven WJ, Voz ML (2002). "Identification of a karyopherin alpha 2 recognition ... 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. ...
... has been shown to interact with KPNA4 and Karyopherin alpha 2. GRCh38: Ensembl release 89: ENSG00000004700 - Ensembl, May ... Seki T, Tada S, Katada T, Enomoto T (1997). "Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1: discrimination ... "Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1: discrimination of Qip1 and Rch1 from hSrp1 by their ability ...
"RanGTP-mediated nuclear export of karyopherin alpha involves its interaction with the nucleoporin Nup153". Proc. Natl. Acad. ... It also acts as the docking site of an importing karyopherin. On the cytoplasmic side of the NPC, Nup358 fulfills an analogous ... Yaseen NR, Blobel G (1997). "Cloning and characterization of human karyopherin beta3". Proc. Natl. Acad. Sci. U.S.A. 94 (9): ... Brownawell AM, Macara IG (2002). "Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding ...
... has been shown to interact with: CIB1, Karyopherin alpha 1, MAPK1, and TOPBP1. GRCh38: Ensembl release 89: ENSG00000104517 ...
... has been shown to interact with: KPNA3, Karyopherin alpha 1, Karyopherin alpha 2, Mothers against decapentaplegic homolog ... Each of these subunits are part of the karyopherin family of proteins. Importin alpha binds the NLS-containing cargo in the ... Moroianu J, Blobel G, Radu A (September 1997). "RanGTP-mediated nuclear export of karyopherin alpha involves its interaction ... Ran-GTP dissociates the karyopherin alphabeta heterodimer by displacing alpha from an overlapping binding site on beta". Proc. ...
Moroianu J, Blobel G, Radu A (September 1997). "RanGTP-mediated nuclear export of karyopherin alpha involves its interaction ... 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): ... Bonifaci N, Moroianu J, Radu A, Blobel G (1997). "Karyopherin beta2 mediates nuclear import of a mRNA binding protein". Proc. ...
"Crystallographic analysis of the recognition of a nuclear localisation signal by the nuclear import factor karyopherin alpha". ... A protein translated with a NLS will bind strongly to importin (aka karyopherin), and, together, the complex will move through ... analysis of the specific yet versatile recognition of distinct nuclear localisation signals by karyopherin alpha". Structure. 8 ... 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 localization signal by the nuclear import factor karyopherin alpha". ... Importin: IPO4, IPO5, IPO7, IPO8, IPO9, IPO11, IPO13 Karyopherin-α: KPNA1, KPNA2, KPNA3, KPNA4, KPNA5, KPNA6 Karyopherin-β: ... Each one of these repeats contains two antiparallel alpha helices linked by a turn, which stack together to form the overall ... Importin-β is the typical structure of a larger superfamily of karyopherins. The basis of their structure is 18-20 tandem ...
"Nuclear localization of the tyrosine kinase Itk and interaction of its SH3 domain with karyopherin alpha (Rch1alpha)". Int. ...
Importin alpha, or karyopherin alpha refers to a class of adaptor proteins that are involved in the import of proteins into the ... Moroianu, J; Blobel, G; Radu, A (1996-06-25). "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 ... Wang, P.; Palese, P.; O'Neill, R. E. (1997-03-01). "The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus ...
2014). "Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear import of ... KPNA proteins have 10 armadillo repeats each consisting of three alpha helices which determine their binding specificity, the ... Additionally, eVP24 inhibits interferon signaling by competitively binding to karyopherins which blocks phosphorylated STAT1 ... "The Ebola virus VP24 protein prevents hnRNP C1/C2 binding to karyopherin α1 and partially alters its nuclear import". J. Infect ...
... 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 alpha subunits, g12-g13 MeSH D12.776.157.325.332.100.200 -- gtp-binding protein alpha subunits, gi-go MeSH ... gtp-binding protein alpha subunits, gq-g11 MeSH D12.776.157.325.332.100.400 -- gtp-binding protein alpha subunits, gs MeSH ... alpha subunit MeSH D12.776.157.057.061.500.500 -- stat1 transcription factor MeSH D12.776.157.057.061.500.750 -- stat2 ...
"Differential regulation of karyopherin alpha 2 expression by TGF-beta1 and IFN-gamma in normal human epidermal keratinocytes: ...
"Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ... The classical karyopherin receptor complex, such as the complex that uses Importin-β1 (encoded by gene KPNB1), is a heterodimer ... However, Transportin-1 can directly bind to the cargo proteins and may not need importin alpha subunit to do it. Transportin-1 ... Bonifaci N, Moroianu J, Radu A, Blobel G (Jun 1997). "Karyopherin beta2 mediates nuclear import of a mRNA binding protein". ...
... a heterodimer of importin alpha and beta subunits also known as karyopherins. Importin alpha binds the NLS-containing cargo in ... Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. Interactions between ... Chook YM, Blobel G (2002). "Karyopherins and nuclear import". Curr. Opin. Struct. Biol. 11 (6): 703-15. doi:10.1016/S0959-440X( ... "Cloning and characterization of human karyopherin beta3". Proc Natl Acad Sci U S A. 94 (9): 4451-6. doi:10.1073/pnas.94.9.4451 ...
First, it is binding importin alpha - another type of karyopherin that binds the cargo protein in the cytoplasm - before the ... 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 ... Karyopherins are a group of proteins involved in transporting molecules between the cytoplasm and the nucleus of a eukaryotic ...
"Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ... Importin subunit alpha-1 is a protein that in humans is encoded by the KPNA1 gene. Karyopherin alpha 1 has been shown to ... "Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import ... Percipalle, P; Clarkson W D; Kent H M; Rhodes D; Stewart M (Mar 1997). "Molecular interactions between the importin alpha/beta ...
"Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ... "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 ...
For example, the beta-karyopherin superfamily consists of alpha solenoid proteins formed from HEAT repeats; importin beta is a ... "alpha alpha superhelix". The CATH database uses the term "alpha horseshoe" for these proteins, and uses "alpha solenoid" for a ... An alpha solenoid (sometimes also known as an alpha horseshoe or as stacked pairs of alpha helices, abbreviated SPAH) is a ... Examples of alpha solenoid structures binding RNA and lipids have also been described. The term "alpha solenoid" has been used ...
Most karyopherins interact directly with their cargo, although some use adaptor proteins.[11] Steroid hormones such as cortisol ... Like the components of other intermediate filaments, the lamin monomer contains an alpha-helical domain used by two monomers to ... Those karyopherins that mediate movement into the nucleus are also called importins, whereas those that mediate movement out of ... macromolecules such as RNA and proteins require association karyopherins called importins to enter the nucleus and exportins to ...
"Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ... Importin subunit alpha-1 is a protein that in humans is encoded by the KPNA1 gene. Karyopherin alpha 1 has been shown to ... "Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import ... Percipalle, P; Clarkson W D; Kent H M; Rhodes D; Stewart M (Mar 1997). "Molecular interactions between the importin alpha/beta ...
"Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ... "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 ...
Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha. ...
Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha. ...
similar to karyopherin (importin) alpha 4 LOC365232 similar to karyopherin (importin) alpha 4 (predicted) predicted is ... similar to karyopherin (importin) alpha 4 (predicted) Symbol and Name status set to provisional. 70820. PROVISIONAL. ...
Synonyms: IPOA3, Importin alpha Q1, Importin subunit alpha-3, Karyopherin subunit alpha-4, MGC12217, ... ... Assignment of KPNA4 and KPNB1 encoding karyopherin alpha 4 and beta 1 to human chromosome bands 11q22 and 17q21 respectively, ... Assignment of KPNA4 and KPNB1 encoding karyopherin alpha 4 and beta 1 to human chromosome bands 11q22 and 17q21 respectively, ... Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1: discrimination of Qip1 and Rch1 from hSrp1 by their ability ...
Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin ... Description: KARYOPHERIN ALPHA protein , Length: 424 No structure alignment results are available for 1EE5.A explicitly.. It is ... YEAST KARYOPHERIN (IMPORTIN) ALPHA IN A COMPLEX WITH A NUCLEOPLASMIN NLS PEPTIDE. ...
Macrocyclic peptide inhibitors for the protein-protein interaction of Zaire Ebola virus protein 24 and karyopherin alpha 5 ... Macrocyclic peptide inhibitors for the protein-protein interaction of Zaire Ebola virus protein 24 and karyopherin alpha 5 X. ...
What is karyopherin alpha 5? Meaning of karyopherin alpha 5 medical term. What does karyopherin alpha 5 mean? ... Looking for online definition of karyopherin alpha 5 in the Medical Dictionary? karyopherin alpha 5 explanation free. ... redirected from karyopherin alpha 5) KPNA5. A gene on chromosome 6q22.1 that encodes an alpha subunit of karyopherin, which ... Karyopherin alpha 5 , definition of karyopherin alpha 5 by Medical dictionary https://medical-dictionary.thefreedictionary.com/ ...
Vega: OTTMUSG3580 (Kpna2, karyopherin (importin) alpha 2)*CCDS: 25565, 25565.1*OMIM: KARYOPHERIN ALPHA-2; KPNA2*Gene Ontology: ... karyopherin (importin) alpha 2. Synonyms: 2410044B12Rik, importin, Importin alpha, importin alpha 1, IPOA1, m-importin, m- ... importin-alpha-P1, pendulin, Rch1. Gene nomenclature, locus information, and GO, OMIM, and PMID associations are updated daily ...
... with endogenous human importins/karyopherins to determine the mechanism of NTM modulation of importin alpha-mediated nuclear ... Targeting Nuclear Import Shuttles, Importins/Karyopherins Alpha by a Peptide Mimicking the NFκB1/p50 Nuclear Localization ... with endogenous human importins/karyopherins to determine the mechanism of NTM modulation of importin alpha-mediated nuclear ...
Meiler, Robert Paul (2010) Die nukleäre Expression von Karyopherin alpha 2: ein prädiktiver Faktor für das Überleben von ... Die nukleäre Expression von Karyopherin alpha 2: ein prädiktiver Faktor für das Überleben von Patientinnen mit ... Karyopherin a2 (KPNA2) has been reported as a important factor of tumorgenesis and progression of breast cancer. The aim of ... Karyopherin α2 (KPNA2) stellte sich als ein wichtiger Faktor bezüglich Tumorentstehung und Fortschreiten des Mammakarzinoms dar ...
... a member of the karyopherin family, plays a vital role in carcinogenesis. Yet its role in colon cancer is poorly characterized ... Karyopherin alpha 2 (KPNA2), a member of the karyopherin family, plays a vital role in carcinogenesis. Yet its role in colon ... Karyopherin alpha 2 is a novel prognostic marker and a potential therapeutic target for colon cancer. *Yu Zhang1. , ... Hu ZY, Yuan SX, Yang Y, Zhou WP, Jiang H. Pleomorphic adenoma gene 1 mediates the role of karyopherin alpha 2 and has ...
Karyopherin Subunit Alpha 6, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The ... a heterodimer of importin alpha and beta subunits also known as karyopherins. Importin alpha binds the NLS-containing cargo in ... KPNA6 (Karyopherin Subunit Alpha 6) is a Protein Coding gene. Diseases associated with KPNA6 include Lennox-Gastaut Syndrome. ... Acetylation of importin-alpha nuclear import factors by CBP/p300. (PMID: 10801418) Bannister AJ … Kouzarides T (Current biology ...
Once inside the CELL NUCLEUS beta karyopherins interact with RAN GTP-BINDING PROTEIN and dissociate from alpha karyopherins. ... Nucleocytoplasmic transport molecules that bind to ALPHA KARYOPHERINS in the CYTOSOL and are involved in transport of molecules ... 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. ... formation by tethering karyopherin alpha 2 and karyopherin beta ...
Importin-alpha is the nuclear import receptor that recognizes cargo proteins carrying conventional basic monopartite and ... alpha Karyopherins / chemistry* * alpha Karyopherins / metabolism Substances * Nuclear Localization Signals * Retinoblastoma ... Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha J Biol Chem. 2003 Jul ... Importin-alpha is the nuclear import receptor that recognizes cargo proteins carrying conventional basic monopartite and ...
Fingerprint Dive into the research topics of Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to ... T1 - Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear import of ... Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear import of ... Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear import of ...
Karyopherin alpha 2 (KPNA2) promotes tumor growth in hepatocellular carcinoma (HCC). We aimed to determine the content and ... Karyopherin alpha 2 (KPNA2) is one of karyopherin a family, and could form heterodimer with Karyopherin 1 to promote nucleus ... Braem CV, Kas K, Meyen E, Debiec-Rychter M, Van De Ven WJ, Voz ML: Identification of a karyopherin alpha 2 recognition site in ... Karyopherin alpha 2 (KPNA2) promotes tumor growth in hepatocellular carcinoma (HCC). We aimed to determine the content and ...
At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta ... "Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ... "Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ... "Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ...
... by the importin-alpha:beta receptor. We now show that Npap60 (also called Nup50), a protein previously believed to be a ... structural component of the NPC, is a Ran binding protein and a cofactor for importin-alpha:be … ... alpha Karyopherins / genetics * alpha Karyopherins / metabolism* * beta Karyopherins / genetics * beta Karyopherins / ... The N terminus binds the C terminus of importin-alpha, while a central domain binds importin-beta. Npap60:importin-alpha:beta ...
At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta ... Karyopherin subunit alpha-4. ,p>This subsection of the ,a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names ... Importin subunit alpha-3Add BLAST. 520. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical view ... Belongs to the importin alpha family.Curated. Keywords - Domaini. Repeat. Phylogenomic databases. evolutionary genealogy of ...
karyopherin (importin) alpha 4 MGI:1100848 .yui-skin-sam .yui-dt th{ background:url(http://www.informatics.jax.org/webshare/ ...
thermophila encodes a large, karyopherin alpha-like protein family. The diagram in panel A depicts the conserved domains of ... Localization studies of 13 putative importin (imp) alpha- and 11 imp beta-like proteins revealed that imp alpha-like proteins ... These data suggest that micronucleus-specific proteins are transported by specific imp alpha adapters. The different imp alpha ... Nucleus-specific importin alpha proteins and nucleoporins regulate protein import and nuclear division in the binucleate ...
BACKGROUND: Karyopherin alpha 2 (KPNA2), a member of the karyopherin family, plays a vital role in carcinogenesis. Yet its role ... karyopherin alpha 2 [RAG cohort 1, importin alpha 1]) and subsequently disturbed the nuclear translocation of TP53 in the GBM ... Karyopherin alpha 2 is a novel prognostic marker and a potential therapeutic target for colon cancer.. J Exp Clin Cancer Res. ... Karyopherin alpha 2 (KPNA2) is a nuclear transport protein upregulated in many cancers. Our previous study has identified KPNA2 ...
Signal transducers and activators of transcription (STAT) utilize karyopherins-alpha (KPNA) for their passage from cytoplasm ... of karyopherin-mediated nuclear transport in the onset and development of DGF. Additionally, it reveals that karyopherins could ... which includes genes encoding for several subtypes of karyopherins, a group of proteins involved in nucleocytoplasmic transport ... Karyopherin-alpha (also known as importin-alpha) is an adaptor protein that recognizes the first discovered or classical NLS, ...
  • Compared with wild-type, passive export rates of a classical karyopherin/importin (Kap) Kap60p/Kap95p-targeted NLS-GFP reporter (cNLS-GFP) were significantly faster in nup188- Δ and nup170- Δ cells. (rupress.org)
  • In yeast and humans, which contain at least 14 and 20 karyopherins, respectively, most are members of the imp β family. (asm.org)
  • Importin-alpha constitutes a multiprotein family in Metazoa with generally similar but perhaps not identical binding specificities ( Mason,2009 ). (eu.org)
  • We detected mRNA of the four karyopherins in normal 3rd day of 5th instar larvae, and in larvae injected with Gram-positive bacteria, Gram-negative bacteria, viruses, and fungi using real-time fluorescence quantitative reverse transcriptase-polymerase chain reaction, and found that the four karyopherins were widely distributed, but their expression levels were related to tissues type, the microbe injected, and the time point. (geneticsmr.com)
  • To identify the import machineries that interact with these different pores, we characterized the large families of karyopherin homologs encoded within the genome. (nih.gov)
  • 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)