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Karyopherin alpha 2

SRP1, Srp1p, Rch1, importin alpha1, Importin alpha, KPNA2, karyopherin alpha2
The import of proteins into the nucleus is a process that involves at least 2 steps. The first is an energy-independent docking of the protein to the nuclear envelope and the second is an energy-dependent translocation through the nuclear pore complex. Imported proteins require a nuclear localization sequence (NLS) which generally consists of a short region of basic amino acids or 2 such regions spaced about 10 amino acids apart. Proteins involved in the first step of nuclear import have been identified in different systems. These include the Xenopus protein importin and its yeast homolog, SRP1 (a suppressor of certain temperature-sensitive mutations of RNA polymerase I in Saccharomyces cerevisiae), which bind to the NLS. KPNA2 protein interacts with the NLSs of DNA helicase Q1 and SV40 T antigen and may be involved in the nuclear transport of proteins. KPNA2 also may play a role in V(D)J recombination [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: importin, CAN, ACID, Alpha-1, V1a
Papers on SRP1
KPNA2 over-expression is a potential marker of prognosis and therapeutic sensitivity in colorectal cancer patients.
Kuwano et al., Maebashi, Japan. In J Surg Oncol, Jan 2016
BACKGROUND: Karyopherin α 2 (KPNA2) is a member of the Karyopherin α family and has recently been reported to play an important role in tumor progression.
Changing expression and subcellular distribution of karyopherins during murine oogenesis.
Holt et al., Newcastle, Australia. In Reproduction, Dec 2015
Of the KPNAs examined (Kpna1, Kpna2, Kpna3, Kpna4, Kpna6, Kpna7, Kpnb1, Ipo5 and Xpo1), all were expressed in the embryonic ovary with up-regulation of protein levels concomitant with meiotic entry for KPNA2, accompanied by the redistribution of the cellular localisation of KPNA2 and XPO1.
Biological versus mineralogical chromium reduction: potential for reoxidation by manganese oxide.
Lan et al., Norman, United States. In Environ Sci Process Impacts, Dec 2015
In this study, Fe-Cr solids were formed by microbial Cr(vi) reduction using Desulfovibrio vulgaris strain RCH1 in the presence of the Fe-bearing minerals hematite, aluminum substituted goethite (Al-goethite), and nontronite (NAu-2, Clay Minerals Society), or by abiotic Cr(vi) reduction by dithionite reduced NAu-2 or iron sulfide (FeS).
Karyopherin Alpha 2 Promotes the Inflammatory Response in Rat Pancreatic Acinar Cells Via Facilitating NF-κB Activation.
Zhang et al., Nantong, China. In Dig Dis Sci, Dec 2015
Karyopherin alpha 2 (KPNA2), a member of the importin α family, reportedly modulates p65 subcellular localization.
MIR517C inhibits autophagy and the epithelial-to-mesenchymal (-like) transition phenotype in human glioblastoma through KPNA2-dependent disruption of TP53 nuclear translocation.
Qi et al., Guangzhou, China. In Autophagy, Nov 2015
Furthermore, following treatment with the autophagy inducer temozolomide (TMZ) and low glucose (LG), MIR517C degraded KPNA2 (karyopherin alpha 2 [RAG cohort 1, importin alpha 1]) and subsequently disturbed the nuclear translocation of TP53 in the GBM cell line U87 in vitro.
Towards elucidating the stability, dynamics and architecture of the nucleosome remodeling and deacetylase complex by using quantitative interaction proteomics.
Vermeulen et al., Nijmegen, Netherlands. In Febs J, May 2015
STRUCTURED DIGITAL ABSTRACT: MBD3 physically interacts with ZNF512B, HDAC1, ZMYND8, GATAD2B, SALL4, GATAD2A, ZNF592, MTA3, ZNF687, CDK2AP1, CHD3, ZNF532, HDAC2, MTA2, CHD4, MTA1, KPNA2, CHD5, RBBP4 and RBBP7 by pull down (View interaction) CDK2AP1 physically interacts with MBD3, MTA3, HDAC2, GATAD2A, CHD4, CDK2AP1, MTA2, HDAC1, MTA1, CHD3, GATAD2B, MBD2, RBBP4 and RBBP7 by pull down (View interaction) MBD3 physically interacts with MTA2, MTA3, RBBP4, RBBP7, HDAC2, HDAC1, CHD4, CHD3 and MTA1 by cross-linking study (View interaction).
Karyopherin alpha 2 is a novel prognostic marker and a potential therapeutic target for colon cancer.
Peng et al., Shanghai, China. In J Exp Clin Cancer Res, 2014
BACKGROUND: Karyopherin alpha 2 (KPNA2), a member of the karyopherin family, plays a vital role in carcinogenesis.
Childhood ovarian malignancy.
Ghorpade et al., Ujjain, India. In J Obstet Gynaecol India, 2014
Immunohistochemistry and newer genetic markers like SALL4 and karyopherin-2 (KPNA2) have been helpful in differentiating ovarian yolk sac tumor from dysgerminoma, teratomas, and other pictures of hepatoid, endometrioid, clear cell carcinomatous, and adenocarcinomatous tissues with varied malignant potential.
The functional role of the novel biomarker karyopherin α 2 (KPNA2) in cancer.
Dyrskjøt et al., Århus, Denmark. In Cancer Lett, 2013
In recent years, Karyopherin α 2 (KPNA2) has emerged as a potential biomarker in multiple cancer forms.
Lymph node dissection in bladder cancer. Impact on staging and prognosis.
Jensen, Århus, Denmark. In Dan Med J, 2012
In evaluation of a molecular marker, KPNA2, we found that the more accurate staging and more favourable prognosis achieved by extended LND compared to a limited LND was essential in evaluation of the prognostic impact of KPNA2.
The interaction between importin-α and Nup153 promotes importin-α/β-mediated nuclear import.
Yoneda et al., Suita, Japan. In Traffic, 2012
importin alpha binds to Nup153
Nuclear import of the yeast hexokinase 2 protein requires α/β-importin-dependent pathway.
Moreno et al., Oviedo, Spain. In J Biol Chem, 2012
Hxk2 as a new cargo for the alpha/beta-importin pathway of S. cerevisiae.
Nuclear retention of importin α coordinates cell fate through changes in gene expression.
Yoneda et al., Ōsaka, Japan. In Embo J, 2012
results collectively reveal that nuclear-localized importin alpha2 influences gene expression and contributes directly to cell fate outcomes including non-apoptotic cell death.
Nuclear transport of Wilms' tumour protein Wt1 involves importins α and β.
Scholz et al., Lübeck, Germany. In Cell Physiol Biochem, 2011
Nuclear translocation of Wilms' tumour protein involves importins alpha and beta, and a nuclear localisation signal in the third zinc finger
Overexpression of Kpnβ1 and Kpnα2 importin proteins in cancer derives from deregulated E2F activity.
Leaner et al., Cape Town, South Africa. In Plos One, 2010
findings suggest that the deregulated activity of E2F in cancer cells causes increased activation of the Kpnbeta1 and Kpnalpha2 promoters, leading to elevated levels of these proteins, and ultimately impacting the cancer phenotype.
Importin KPNA2, NBS1, DNA repair and tumorigenesis.
Kao et al., Taipei, Taiwan. In J Mol Histol, 2006
This review focuses on recent experimental evidences demonstrating how NBS1 is translocated into the nucleus by an importin KPNA2 which mediates NBS1 subcellular localization and the functions of the NBS1 complex in tumorigenesis.
Importin provides a link between nuclear protein import and U snRNA export.
Izaurralde et al., Heidelberg, Germany. In Cell, 1996
We find approximately 30% of SRP1p, the yeast importin-alpha, in a nuclear complex with the Saccharomyces cerevisiae nuclear cap-binding protein complex (CBC).
Localization, interaction, and RNA binding properties of the V(D)J recombination-activating proteins RAG1 and RAG2.
Baltimore et al., New York City, United States. In Immunity, 1995
The RAG1 interacting proteins SRP1 and Rch1 directly bind to the nuclear localization signals of RAG1, which mediate the nuclear and nucleolar translocation of the protein.
Distinct functions for the two importin subunits in nuclear protein import.
Laskey et al., Cambridge, United Kingdom. In Nature, 1995
Importin-alpha is primarily responsible for NLS recognition and is a member of a protein family that includes the essential yeast nuclear pore protein SRP1p (ref.
Isolation of a protein that is essential for the first step of nuclear protein import.
Hartmann et al., Cambridge, United Kingdom. In Cell, 1995
Importin shows 44% sequence identity with SRP1p, a protein associated with the yeast nuclear pore complex.
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