<b><i>Introduction:</i></b> Karyopherin alpha 2 (KPNA2) and karyopherin beta 1 (KPNB1) constitute nuclear transport protein complexes involved in nuclear import and are significant in tumor progression. Although high KPNA2 expression was associated with poor prognosis in solid tumors, the relationship between KPNA2 and KPNB1 ...
Yoshihito Ohhara +10 more
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KPNB1 (karyopherin (importin) beta 1) [PDF]
Review on KPNB1 (karyopherin (importin) beta 1), with data on DNA, on the protein encoded, and where the gene is implicated.
Maria Giubettini +5 more
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The binding site of karyopherin alpha for karyopherin beta overlaps with a nuclear localization sequence. [PDF]
By using proteolysis, recombinant mutant proteins, or synthetic peptides and by testing these reagents in liquid phase binding or nuclear import assays, we have mapped binding regions of karyopherin alpha. We found that the C-terminal region of karyopherin alpha recognizes the nuclear localization sequence (NLS), whereas its N-terminal region binds ...
J, Moroianu, G, Blobel, A, Radu
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Inhibition of Karyopherin beta 1 suppresses prostate cancer growth [PDF]
Prostate cancer (PCa) initiation and progression requires activation of numerous oncogenic signaling pathways. Nuclear-cytoplasmic transport of oncogenic factors is mediated by Karyopherin proteins during cell transformation. However, the role of nuclear transporter proteins in PCa progression has not been well defined.
Yang, Jian +11 more
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Evolutionary and Transcriptional Analysis of Karyopherin β Superfamily Proteins [PDF]
In eukaryotes, karyopherin beta superfamily proteins mediate nucleocytoplasmic transport of macromolecules. We investigated the evolutionary and transcriptional patterns of these proteins using bioinformatics approaches. No obvious homologs were found in prokaryotes, but an extensive set of beta-karyopherin proteins was found in yeast.
Quan, Y. +4 more
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Karyopherin β2B participates in mRNA export from the nucleus [PDF]
Transport of macromolecules between the cell nucleus and cytoplasm occurs through the nuclear pores and is mediated by soluble carriers known as karyopherins (Kaps), transportins, importins, or exportins. We report that Kap β2B (transportin-2) forms complexes with the mRNA export factor TAP in the presence of RanGTP, as shown by ...
Monee K, Shamsher +2 more
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Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes. [PDF]
Previously, we had purified a cytosolic protein complex, termed karyopherin, that functions in docking import substrate at the nuclear envelope in digitonin-permeabilized cells and also had molecularly cloned and sequenced its 97-kDa beta subunit. We now report that the karyopherin alpha subunit is the previously identified protein NPI-1/SRP-1 of ...
J, Moroianu, G, Blobel, A, Radu
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Disassembly of RanGTP-Karyopherin β Complex, an Intermediate in Nuclear Protein Import [PDF]
We previously showed that RanGTP forms a 1:1 complex with karyopherin beta that renders RanGTP inaccessible to RanGAP (Floer, M., and Blobel, G. (1996) J. Biol. Chem. 271, 5313-5316) and karyopherin beta functionally inactive (Rexach, M., and Blobel, G. (1995) Cell 83, 683-692).
M, Floer, G, Blobel, M, Rexach
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Ran-binding Protein 1 (RanBP1) Forms a Ternary Complex with Ran and Karyopherin β and Reduces Ran GTPase-activating Protein (RanGAP) Inhibition by Karyopherin β [PDF]
The nuclear accumulation of proteins containing nuclear localization signals requires the Ran GTPase and a complex of proteins assembled at the nuclear pore. RanBP1 is a cytosolic Ran-binding protein that inhibits RCC1-stimulated release of GTP from Ran. RanBP1 also promotes the binding of Ran to karyopherin beta (also called importin beta and p97) and
K M, Lounsbury, I G, Macara
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Remodeling of the pioneer translation initiation complex involves translation and the karyopherin importin β [PDF]
Mammalian mRNAs lose and acquire proteins throughout their life span while undergoing processing, transport, translation, and decay. How translation affects messenger RNA (mRNA)–protein interactions is largely unknown. The pioneer round of translation uses newly synthesized mRNA that is bound by cap-binding protein 80 (CBP80)–CBP20 (also known as the ...
Hanae, Sato, Lynne E, Maquat
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