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.
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 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.
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.
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.
Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.
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 is a basic helix-loop-helix transcription factor that is regulated by OXYGEN availability and is targeted for degradation by VHL TUMOR SUPPRESSOR PROTEIN.
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.
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.
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.
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.
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 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.
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.
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.
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.
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 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.

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 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: 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. doi: ...
"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 ...
... also known as karyopherin subunit alpha-3 is a protein that in humans is encoded by the KPNA3 gene. ... "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 ...
... , also known as karyopherin subunit alpha-4, is a protein that in humans is encoded by the KPNA4 gene. ... "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 ... Seki T, Tada S, Katada T, Enomoto T (May 1997). "Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1: ...
... 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 ...
"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 ...
Moroianu J, Blobel G, Radu A (1997). "RanGTP-mediated nuclear export of karyopherin alpha involves its interaction with the ... 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 an 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 localisation signal by the nuclear import factor karyopherin alpha". ... The broad outline of this model was confirmed ten years later by the crystallographic analysis of importin alpha complexed with ...
"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: ... Importin is a type of karyopherin that transports protein molecules from the cell's cytoplasm to the nucleus. It does so by ... Each one of these repeats contains two antiparallel alpha helices linked by a turn, which stack together to form the overall ...
"Nuclear localization of the tyrosine kinase Itk and interaction of its SH3 domain with karyopherin alpha (Rch1alpha)". Int. ...
"Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal ... "Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import ... Importin subunit alpha-5 is a protein that in humans is encoded by the KPNA1 gene. Importin subunit alpha-5 has been shown to ... Percipalle, P; Clarkson W D; Kent H M; Rhodes D; Stewart M (Mar 1997). "Molecular interactions between the importin alpha/beta ...
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 (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 ... Wang, P.; Palese, P.; O'Neill, R. E. (1 March 1997). "The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus ...
August 2014). "Ebola virus VP24 targets a unique NLS binding site on karyopherin alpha 5 to selectively compete with nuclear ... 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". The ...
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 proteins involved in transporting molecules between the cytoplasm and the nucleus of a eukaryotic cell. The ...
... 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: ...
... 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 ... May 2020). "X-ray Structure of the Human Karyopherin RanBP5, an Essential Factor for Influenza Polymerase Nuclear Trafficking ... Yaseen NR, Blobel G (April 1997). "Cloning and characterization of human karyopherin beta3". Proceedings of the National ...
"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". ...
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 ...
... karyopherins MeSH D12.776.543.585.750.500.100 - alpha karyopherins MeSH D12.776.543.585.750.500.249 - beta karyopherins MeSH ... gtp-binding protein alpha subunit, gi2 MeSH D12.776.543.325.100.300 - gtp-binding protein alpha subunits, gq-g11 MeSH D12.776. ... alpha-1 MeSH D12.776.543.750.720.300.300.300.300.200 - receptors, adrenergic, alpha-2 MeSH D12.776.543.750.720.300.300.300.340 ... alpha MeSH D12.776.543.750.070.300.300.300.700 - receptors, adrenergic, alpha-1 MeSH D12.776.543.750.070.300.300.300.725 - ...
Karyopherin beta2 (transportin), a riboprotein transporter also interacts with p62. P62 also interacts with Nup93, and when ... This protein associates with the importin alpha/beta complex which is involved in the import of proteins containing nuclear ... 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- ...
A HEAT repeat is a protein tandem repeat structural motif composed of two alpha helices linked by a short loop. HEAT repeats ... Representative examples of HEAT repeat proteins include importin β (also known as karyopherin β) family, regulatory subunits of ... "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 nucleoporin Nup98 is a site for GDP/GTP exchange on ran and termination of karyopherin beta 2-mediated nuclear import". The ... "Identification of nuclear-import and cell-cycle regulatory proteins that bind to prothymosin alpha". Biochemistry and Cell ... karyopherin alpha3/Qip". The Journal of Biological Chemistry. 275 (14): 10099-104. doi:10.1074/jbc.275.14.10099. PMID 10744690 ...
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 ... such as TNF alpha or GM-CSF. It has been demonstrated that given complete complementarity between the miRNA and target mRNA ... adipogenesis requires a peroxisome proliferator-activated receptor-gamma-associated repression of HDAC1 at the C/ebp alpha gene ...
Though both isoforms contain the NLS, the sequence in DUT-M is sequestered away from cognate karyopherins. The isoelectric ... and identification of rat deoxyuridine triphosphatase as an inhibitor of peroxisome proliferator-activated receptor alpha". The ...
Those karyopherins that mediate movement into the nucleus are also called importins, whereas those that mediate movement out of ... Like the components of other intermediate filaments, the lamin monomer contains an alpha-helical domain used by two monomers to ... Most karyopherins interact directly with their cargo, although some use adaptor proteins. Steroid hormones such as cortisol and ... October 2007). "LPS-induced down-regulation of signal regulatory protein {alpha} contributes to innate immune activation in ...
Shamsher MK, Ploski J, Radu A (2002). "Karyopherin beta 2B participates in mRNA export from the nucleus". Proc. Natl. Acad. Sci ... Percipalle P, Clarkson WD, Kent HM, Rhodes D, Stewart M (1997). "Molecular interactions between the importin alpha/beta ... Ran is involved in the transport of proteins across the nuclear envelope by interacting with karyopherins and changing their ... Chook YM, Blobel G (1999). "Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp". Nature. 399 (6733): 230 ...
The Tap-C domain is made of four alpha helices packed against each other. The arrangement of helices 1, 2 and 3 is similar to ... Shamsher MK, Ploski J, Radu A (October 2002). "Karyopherin beta 2B participates in mRNA export from the nucleus". Proceedings ...
... including karyopherins 1.I.2 Plant plasmodesmata family 2.A.1 Major Facilitator superfamily (MFS), see also Lactose permease, ... Family 1.D.60 The Alpha,Gamma-Cyclic Peptide (AGCP) Family 1.D.61 The Anionophoric 2,6-Bis(Benzimidazol-2-yl)Pyridine (ABBP) ... Family 1.D.53 The alpha, gamma-Peptide Nanotube (a,gPepNT) Family 1.D.54 The potassium-selective Hexyl-Benzoureido-15-Crown-5- ... Ether Ion Channel (HBEC) Family 1.D.55 The Porphyrin-based Nanopore (PorNP) Family 1.D.56 The Alpha-Aminoisobutyrate (Aib) ...
... this family is further subdivided to the karyopherin-α and the karyopherin-β subfamilies. Other nuclear transport receptors ... About half of the nucleoporins typically contain solenoid protein domains-either an alpha solenoid or a beta-propeller fold, or ... The largest family of nuclear transport receptors are karyopherins, which includes dozens of both importins and exportins; ...
Studies of SARS-CoV report this may be mediated by binding of ORF6 protein to karyopherins. In SARS-CoV-2, the ORF6 protein ... It has an amphipathic N-terminal alpha helix that associates with the membrane, but is not a transmembrane protein. Its ... reportedly interacts with RAE1 and NUP98, blocking karyopherin interactions. Liu, Ding Xiang; Fung, To Sing; Chong, Kelvin Kian ...
... alpha 1 Interleukin 13 receptor, alpha 1 Karyopherin alpha 1 Laminin, alpha 1 Major histocompatibility complex, class II, DP ... alpha 1 collagen, type II, alpha 1 Collagen, type III, alpha 1 Collagen, type IV, alpha 1 Collagen, type V, alpha 1 Collagen, ... type VI, alpha 1 Collagen, type VII, alpha 1 Collagen, type VIII, alpha 1 Collagen, type IX, alpha 1 Collagen, type X, alpha 1 ... alpha 1 Collagen, type XIII, alpha 1 Collagen, type XIV, alpha 1 Collagen, type XV, alpha 1 Collagen, type XVI, alpha 1 ...
Binds to and disrupts nuclear import complex formation by tethering karyopherin alpha 2 and karyopherin beta 1 to the membrane ...
KARYOPHERIN ALPHA (YEAST) + SV40 T ANTIGEN NLS. 1ee4. CRYSTAL STRUCTURE OF YEAST KARYOPHERIN (IMPORTIN) ALPHA IN A COMPLEX WITH ... Mouse Importin alpha-bipartite NLS from human retinoblastoma protein Complex. 1pjn. Mouse Importin alpha-bipartite NLS N1N2 ... Mouse Importin alpha- phosphorylated SV40 CN peptide complex. 1q1t. Mouse Importin alpha: non-phosphorylated SV40 CN peptide ... YEAST KARYOPHERIN (IMPORTIN) ALPHA IN A COMPLEX WITH A NUCLEOPLASMIN NLS PEPTIDE. ...
alpha Karyopherins Entry term(s). Importin-alpha Karyopherin alpha Karyopherins, alpha NLS Receptor NLS-Binding Protein NLSBP ... Cariophérines alpha Entry term(s):. Importin-alpha. Karyopherin alpha. Karyopherins, alpha. NLS Receptor. NLS-Binding Protein. ... 2002; KARYOPHERIN ALPHA (now ALPHA KARYOPHERINS) was indexed under NUCLEAR PROTEINS 1994-2001; IMPORTIN-ALPHA was indexed under ... 2002; use ALPHA KARYOPHERINS (NM) 1994-2001; for IMPORTIN-ALPHA use KARYOPHERINS 1995-2001; for NLS-BINDING PROTEIN, NLSBP & ...
Carrier Proteins - alpha Karyopherins PubMed MeSh Term * Carrier Proteins - beta Karyopherins PubMed MeSh Term ... Carrier Proteins - Karyopherins PubMed MeSh Term *Overview. Overview. subject area of * A putative N-terminal nuclear export ...
Karyopherin Alpha 2 Promotes the Inflammatory Response in Rat Pancreatic Acinar Cells Via Facilitating NF-κB Activation. ... Plasma contents of tumor necrosis factor-alpha (TNF-alpha) and interleukin-6 (IL-6) and biochemistry indexes were determined. ... Karyopherin alpha 2 (KPNA2), a member of the importin α family, reportedly modulates p65 subcellular localization. AIM: This ... RESULTS: After the treatment, the levels of TNF-alpha and IL-6 were significantly decreased in both groups (all P. ...
Karyopherin alpha use alpha Karyopherins Karyopherin beta use beta Karyopherins Karyopherin beta Subunit use beta Karyopherins ... Karyopherin-beta Subunit use beta Karyopherins Karyopherins Karyopherins, alpha use alpha Karyopherins ...
Human KPNa2(Karyopherin Alpha 2) ELISA Kit. *Human KRAS(V-Ki-Ras2 Kirsten Rat Sarcoma Viral Oncogene Homolog) ELISA Kit ... Human CHRNa1(Cholinergic Receptor, Nicotinic, Alpha 1) ELISA Kit. *Human CHRNa3(Cholinergic Receptor, Nicotinic, Alpha 3) ELISA ... Human CHRNa1(Cholinergic Receptor, Nicotinic, Alpha 1) ELISA Kit. *Human CHRNa3(Cholinergic Receptor, Nicotinic, Alpha 3) ELISA ... Human IFNa10(Interferon Alpha 10) ELISA Kit. *Human IkBKb(Inhibitor Of Kappa-Light Polypeptide Gene Enhancer In B-Cells Kinase ...
Human KPNa2(Karyopherin Alpha 2) ELISA Kit. *Human KRT14(Keratin 14) ELISA Kit ... Human IFNa2(Interferon Alpha 2) ELISA Kit. *Human IGFALS(Insulin Like Growth Factor Binding Protein, Acid Labile Subunit) ELISA ... Human IFNa2(Interferon Alpha 2) ELISA Kit. *Human IGFALS(Insulin Like Growth Factor Binding Protein, Acid Labile Subunit) ELISA ... Mouse LRG1(Leucine Rich Alpha-2-Glycoprotein 1) ELISA Kit. *Mouse LRP1(Low Density Lipoprotein Receptor Related Protein 1) ...
Human KPNa2(Karyopherin Alpha 2) ELISA Kit. *Human KRT14(Keratin 14) ELISA Kit ... Human IFNa2(Interferon Alpha 2) ELISA Kit. *Human IGFALS(Insulin Like Growth Factor Binding Protein, Acid Labile Subunit) ELISA ... Human IFNa2(Interferon Alpha 2) ELISA Kit. *Human IGFALS(Insulin Like Growth Factor Binding Protein, Acid Labile Subunit) ELISA ... Mouse LRG1(Leucine Rich Alpha-2-Glycoprotein 1) ELISA Kit. *Mouse LRP1(Low Density Lipoprotein Receptor Related Protein 1) ...
... domain of importin alpha by importin beta is critical for the nuclear import of protein cargoes containing a classical nuclear ... Molecular recognition of the importin beta-binding (IBB) domain of importin alpha by importin beta is critical for the nuclear ... beta Karyopherins * Tryptophan Grant support * GM 41955/GM/NIGMS NIH HHS/United States ...
Human FUCa2(Fucosidase Alpha L2, Plasma) ELISA Kit. *Human GABARAPL2(GABA-A Receptor Associated Protein Like Protein 2) ELISA ... Human KPNb1(Karyopherin Beta) ELISA Kit. *Human KRT12(Keratin 12) ELISA Kit ... Mouse REG1a(Regenerating Islet Derived Protein 1 Alpha) ELISA Kit. *Mouse SIGLEC3(Sialic Acid Binding Ig Like Lectin 3) ELISA ... Human HNF1a(Hepatocyte Nuclear Factor 1 Alpha) ELISA Kit. *Human HSD17b1(17-Beta-Hydroxysteroid Dehydrogenase Type 1) ELISA Kit ...
Human FUCa2(Fucosidase Alpha L2, Plasma) ELISA Kit. *Human GABARAPL2(GABA-A Receptor Associated Protein Like Protein 2) ELISA ... Human KPNb1(Karyopherin Beta) ELISA Kit. *Human KRT12(Keratin 12) ELISA Kit ... Mouse REG1a(Regenerating Islet Derived Protein 1 Alpha) ELISA Kit. *Mouse SIGLEC3(Sialic Acid Binding Ig Like Lectin 3) ELISA ... Human HNF1a(Hepatocyte Nuclear Factor 1 Alpha) ELISA Kit. *Human HSD17b1(17-Beta-Hydroxysteroid Dehydrogenase Type 1) ELISA Kit ...
2013b). MERS-CoV 4b protein interferes with NF-κB-mediated innate immune response by binding karyopherin-α4 (KPNA4), thus ... Herpes simplex virus 1 E3 ubiquitin ligase ICP0 protein inhibits tumor necrosis factor alpha-induced NF-κB activation by ...
Collagen alpha-1(XXVIII)Rabbit Polyclonal Antibody. *Collagen I Rabbit Polyclonal Antibody ... Karyopherin α2 Rabbit Polyclonal Antibody. *KChIP1 Rabbit Polyclonal Antibody. *KChIP3 Rabbit Polyclonal Antibody ...
karyopherin (importin) alpha 2. G3BP2. 94913_at. Ras-GTPase-activating protein (GAP120) SH3-domain binding protein 2. ... Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. ... Gene expression profile induced by 17 alpha-ethynyl estradiol in the prepubertal female reproductive system of the rat. Toxicol ... complement component 1, q subcomponent, alpha polypeptide. C1QB. 96020_at. complement component 1, q subcomponent, beta ...
Both far-western analyses and immuno-pull-down assays indicate interaction of APE1 with karyopherin alpha 1 and 2, which ...
alpha Karyopherins / analysis Actions. * Search in PubMed * Search in MeSH * Add to Search ...
Significance of karyopherin-{alpha} 2 (KPNA2) expression in esophageal squamous cell carcinoma.. Sakai M; Sohda M; Miyazaki T; ... Significance of immunohistochemical expression of estrogen receptors alpha and beta in squamous cell carcinoma of the esophagus ...
... a heterodimer of importin alpha and beta subunits also known as karyopherins. Importin alpha binds the NLS-containing cargo in ... karyopherin subunit alpha-6. Description. From NCBI Gene: Nucleocytoplasmic transport, a signal- and energy-dependent process, ... Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. The protein encoded by ... this gene is a member of the importin alpha family. [provided by RefSeq, Jul 2008] ...
2002; KARYOPHERIN ALPHA (now ALPHA KARYOPHERINS) was indexed under NUCLEAR PROTEINS 1994-2001; IMPORTIN-ALPHA was indexed under ... Karyopherins [D12.776.157.530.750.500] * alpha Karyopherins [D12.776.157.530.750.500.100] * beta Karyopherins [D12.776.157.530. ... Karyopherins [D12.776.543.585.750.500] * alpha Karyopherins [D12.776.543.585.750.500.100] * beta Karyopherins [D12.776.543.585. ... 2002; use ALPHA KARYOPHERINS (NM) 1994-2001; for IMPORTIN-ALPHA use KARYOPHERINS 1995-2001; for NLS-BINDING PROTEIN, NLSBP & ...
Disease-specific alteration of karyopherin-alpha 4 subtype establishes feed-forward oncogenic signaling in squamous cell ... Immortalized human hepatocyte (IHH) mRNA response to interferon alpha treatment. GSE72206. Comparative Gene Profiling Study ... CCAAT/enhancer-binding protein alpha is epigenetically silenced by histone acetylation in endometriosis and promotes the ... Primary human lung microvascular endothelial cells treated with universal interferon alpha beta or interferon gamma. ...
alpha Karyopherins Entry term(s). Importin-alpha Karyopherin alpha Karyopherins, alpha NLS Receptor NLS-Binding Protein NLSBP ... Cariophérines alpha Entry term(s):. Importin-alpha. Karyopherin alpha. Karyopherins, alpha. NLS Receptor. NLS-Binding Protein. ... 2002; KARYOPHERIN ALPHA (now ALPHA KARYOPHERINS) was indexed under NUCLEAR PROTEINS 1994-2001; IMPORTIN-ALPHA was indexed under ... 2002; use ALPHA KARYOPHERINS (NM) 1994-2001; for IMPORTIN-ALPHA use KARYOPHERINS 1995-2001; for NLS-BINDING PROTEIN, NLSBP & ...
2002; KARYOPHERIN ALPHA (now ALPHA KARYOPHERINS) was indexed under NUCLEAR PROTEINS 1994-2001; IMPORTIN-ALPHA was indexed under ... Karyopherins [D12.776.157.530.750.500] * alpha Karyopherins [D12.776.157.530.750.500.100] * beta Karyopherins [D12.776.157.530. ... Karyopherins [D12.776.543.585.750.500] * alpha Karyopherins [D12.776.543.585.750.500.100] * beta Karyopherins [D12.776.543.585. ... 2002; use ALPHA KARYOPHERINS (NM) 1994-2001; for IMPORTIN-ALPHA use KARYOPHERINS 1995-2001; for NLS-BINDING PROTEIN, NLSBP & ...
... alpha 1-Antitrypsin N0000169495 alpha Catenin N0000169678 alpha Karyopherins N0000170004 alpha-2-Antiplasmin N0000183458 alpha- ... alpha-Galactosidase N0000178561 alpha-Globins N0000007645 Alpha-Globulins N0000167711 alpha-Glucosidases N0000167712 alpha-L- ... alpha-Macroglobulins N0000167728 alpha-Mannosidase N0000005770 alpha-Methyltyrosine N0000170379 alpha-MSH N0000167718 alpha-N- ... alpha-Crystallins N0000168521 alpha-Cyclodextrins N0000170294 alpha-Defensins N0000170405 alpha-Endorphin N0000171366 alpha- ...
HN - 2002; use ALPHA KARYOPHERINS (NM) 1994-2001; for IMPORTIN-ALPHA use KARYOPHERINS 1995-2001; for NLS-BINDING PROTEIN, NLSBP ... Karyopherins are heteromeric molecules composed two major types of components, ALPHA KARYOPERINS and BETA KARYOPHERINS, that ... Once inside the CELL NUCLEUS beta karyopherins interact with RAN GTP-BINDING PROTEIN and dissociate from alpha karyopherins. ... HN - 2002; use BETA KARYOPHERINS (NM) 1995-2001; for IMPORTIN-BETA use KARYOPHERINS (NM) 1995-2001 BX - Karyopherin-beta MH - ...
Expression levels of UCA1, microRNA (miR)-671-5p, and KPNA4 (karyopherin subunit alpha 4) mRNA were detected using quantitative ... PD pathological changes, such as neuronal apoptosis and the intraneuronal alpha-synuclein aggregation, can be reproduced in the ... Parkinsons disease (PD) is associated with dopaminergic neuron loss and alpha-synuclein aggregation caused by ROS ... transfection of the alpha-synuclein wild-type or mutant gene, genetic manipulation of other genes involved in PD). In addition ...
The karyopherin receptor complex is a heterodimer of an alpha subunit which recognizes the nuclear localization signal and a ... This gene encodes the beta subunit of the karyopherin receptor complex which interacts with nuclear localization signals to ...
... irrationality britannia s267 s265 s263 s262 s261 primaria metasilicate virginia s259 s258 inhabitant s255 karyopherin s253 s252 ... hemorrhagica hedonistic rsba colombia alpk1 rsc8 rsc2 unauthorized rsal rsai perseverance rsaa acetylneuraminate rsb1 alpha ... sordellii pexiganan reach virginity hedysarum lamberts phonemic ringer ovicidal gentiobiosyl ringed tirilazad karyopherins ... piperidylidene acetylation emotive caenocholax wilcoxii platysternon syrup esha acetylating hydroxypipecolic alphav alphas ...
  • 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. (nih.gov)
  • 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. (nih.gov)
  • Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. (nih.gov)
  • The protein encoded by this gene is a member of the importin alpha family. (nih.gov)
  • Inside the CELL NUCLEUS alpha karyopherins dissociate from beta karypherins and their cargo. (nih.gov)
  • Once attached to their cargo they bind to BETA KARYOPHERINS and are transported through the NUCLEAR PORE COMPLEX . (nih.gov)
  • ORF6 protein (open reading fram 6): Binds to and disrupts nuclear import complex formation by tethering karyopherin alpha 2 and karyopherin beta 1 to the membrane. (godlikeproductions.com)
  • Ya en el interior del NUCLEO CELULAR, las alfa carioferinas se disocian de las beta carioferinas y su transporte. (bvsalud.org)
  • Karyopherin beta, mediates nuclear import of ribosomal proteins prior to assembly into ribosomes and. (yeastrc.org)
  • In plakoglobin arm repeats bind alpha-catenin and N-cadherin. (embl.de)
  • Armadillo-like helical domain containing , aka the Armadillo-like helical superfamily , is a domain consisting of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed superhelix, where the repeats that make up this structure are arranged about a common axis. (wellnessadvantage.com)
  • 16. Identification of karyopherin-alpha 2 as an Oct4 associated protein. (nih.gov)
  • Here, we show that an early step of HIV-1 nuclear import is the recognition of the MA nuclear localization signal (NLS) by Rch1, a member of the karyopherin-alpha family. (nih.gov)
  • These results are consistent with a model in which Rch1 or another member of the karyopherin-alpha family, through the recognition of the MA NLS, participates in docking the HIV-1 nucleoprotein complex at the nuclear pore. (nih.gov)
  • Both far-western analyses and immuno-pull-down assays indicate interaction of APE1 with karyopherin alpha 1 and 2, which requires the 20 N-terminal residues and implicates nuclear importins in APE1's nuclear translocation. (nih.gov)
  • Moreover, SARS-CoV-2 ORF6 inhibits NLRC5 function via blocking karyopherin complex-dependent nuclear import of NLRC5. (nature.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. (nih.gov)
  • 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. (nih.gov)
  • Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. (nih.gov)
  • The protein encoded by this gene is a member of the importin alpha family. (nih.gov)
  • Once attached to their cargo they bind to BETA KARYOPHERINS and are transported through the NUCLEAR PORE COMPLEX . (bvsalud.org)