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NMD3 Nmd3p

NMD3, Nmd3p, hNMD3
Ribosomes are composed of 60S and 40S subunits that are assembled in the nucleolus and exported to the cytoplasm through nuclear pore complexes in the nuclear envelope. NMD3 is an adaptor for 60S subunit export via the CRM1 (XPO1; MIM 602559) pathway (Trotta et al., 2003 [PubMed 12773398]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: CRM1, CAN, RAN, STEP, HAD
Papers on NMD3
NMD3 regulates both mRNA and rRNA nuclear export in African trypanosomes via an XPOI-linked pathway.
New
Matthews et al., Bern, Switzerland. In Nucleic Acids Res, Jun 2015
Ribosomal RNAs must also be exported from the nucleus and the trypanosome orthologue of NMD3 has been confirmed to be involved in rRNA processing and export, matching its function in other organisms.
Analysis of several loci from genome-wide association studies in Parkinson's disease in mainland China.
New
Tang et al., Changsha, China. In Neurosci Lett, Mar 2015
However, we did not observe any significant difference in genotype or allele distribution between PD and control for rs34016896 in NMD3 and rs6812193 in STBD1.
Retention of OsNMD3 in the cytoplasm disturbs protein synthesis efficiency and affects plant development in rice.
Zhou et al., Beijing, China. In J Exp Bot, 2014
This study chose a highly conserved trans-factor, the 60S ribosomal subunit nuclear export adaptor NMD3, to characterize the mechanism of ribosome biogenesis in the monocot plant Oryza sativa (rice).
Association of Parkinson disease risk loci with mild parkinsonian signs in older persons.
De Jager et al., Boston, United States. In Jama Neurol, 2014
In the autopsy cohort, only NMD3 (rs34016896; Pā€‰=ā€‰.03) was related to nigral neuronal loss, and no associations were detected with Lewy bodies.
CRM1 and its ribosome export adaptor NMD3 localize to the nucleolus and affect rRNA synthesis.
Laiho et al., Baltimore, United States. In Nucleus, 2013
CRM1 is an export factor that together with its adaptor NMD3 transports numerous cargo molecules from the nucleus to cytoplasm through the nuclear pore.
Arabidopsis NMD3 is required for nuclear export of 60S ribosomal subunits and affects secondary cell wall thickening.
Bai et al., Beijing, China. In Plos One, 2011
NMD3 is required for nuclear export of the 60S ribosomal subunit in yeast and vertebrate cells, but no corresponding function of NMD3 has been reported in plants.
Characterization of the nuclear export adaptor protein Nmd3 in association with the 60S ribosomal subunit.
GeneRIF
Frank et al., Albany, United States. In J Cell Biol, 2010
cryo-EM reconstruction of the 60S subunit in complex with Nmd3; is attached to the regions around helices 38, 69, and 95 of the 25S rRNA
Arx1 is a nuclear export receptor for the 60S ribosomal subunit in yeast.
Johnson et al., Austin, United States. In Mol Biol Cell, 2008
We previously showed that nuclear export of the large (60S) ribosomal subunit relies on Nmd3 in a Crm1-dependent manner.
Mapping the functional domains of yeast NMD3, the nuclear export adapter for the 60 S ribosomal subunit.
GeneRIF
Johnson et al., Austin, United States. In J Biol Chem, 2007
analysis of the functional domains of yeast NMD3, the nuclear export adapter for the 60 S ribosomal subunit
Nup214-Nup88 nucleoporin subcomplex is required for CRM1-mediated 60 S preribosomal nuclear export.
Fornerod et al., Amsterdam, Netherlands. In J Biol Chem, 2006
Export of the preribosomal 60 S subunit follows this pathway through the adaptor protein NMD3.
Defining the order in which Nmd3p and Rpl10p load onto nascent 60S ribosomal subunits.
Johnson et al., Austin, United States. In Mol Cell Biol, 2005
We have recently shown that Rpl10p as well as the cytoplasmic GTPase Lsg1p are required for releasing the 60S nuclear export adapter Nmd3p from subunits in the cytoplasm.
Release of the export adapter, Nmd3p, from the 60S ribosomal subunit requires Rpl10p and the cytoplasmic GTPase Lsg1p.
GeneRIF
Johnson et al., Austin, United States. In Embo J, 2005
correct loading of Rpl10p into 60S subunits is required for the release of Nmd3p from subunits by Lsg1p
Functional interaction in establishment of ribosomal integrity between small subunit protein rpS6 and translational regulator rpL10/Grc5p.
Koller et al., Salzburg, Austria. In Fems Yeast Res, 2004
Here, we report that rpL10/Grc5p functionally interacts with the nuclear export factor Nmd3p in modulation of the cellular polysome complement and with the small subunit protein rpS6 in subunit joining and differential protein expression.
Coordinated nuclear export of 60S ribosomal subunits and NMD3 in vertebrates.
GeneRIF
Dahlberg et al., Madison, United States. In Embo J, 2003
contains a CRM-1-dependent leucine-rich nuclear export signal and a complex, dispersed nuclear localization signal (NMD3)
The putative GTPases Nog1p and Lsg1p are required for 60S ribosomal subunit biogenesis and are localized to the nucleus and cytoplasm, respectively.
Johnson et al., Austin, United States. In Mol Cell Biol, 2003
We characterized two essential putative GTPases, Nog1p and Lsg1p, that are found associated with free 60S ribosomal subunits affinity purified with the nuclear export adapter Nmd3p.
Nuclear export of ribosomal subunits.
Review
Dahlberg et al., Austin, United States. In Trends Biochem Sci, 2002
Export of the large (60S) subunit requires a shuttling adaptor protein, NMD3, which binds to mature, correctly folded subunits.
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