TY - JOUR
T1 - Upf1p, a highly conserved protein required for nonsense-mediated mRNA decay, interacts with the nuclear pore proteins Nup100p and Nup116p
AU - Nazarenus, Tara
AU - Cedarberg, Rebecca
AU - Bell, Ryan
AU - Cheatle, Joseph
AU - Forch, Amanda
AU - Haifley, Alexis
AU - Hou, Ann
AU - Kebaara, Bessie Wanja
AU - Shields, Christina
AU - Stoysich, Kate
AU - Taylor, Rachel
AU - Atkin, Audrey L.
N1 - Funding Information:
This work was supported by National Science Foundation under grant 9874516 and by grants from the University of Nebraska-Lincoln Research Council and Nebraska EPSCoR. Any opinion, finding, and conclusion, or recommendation expressed in this material is that of the authors and does not necessarily reflect the views of the National Science Foundation, University of Nebraska-Lincoln Research Council or Nebraska EPSCoR.
PY - 2005/1/31
Y1 - 2005/1/31
N2 - Saccharomyces cerevisiae Upf1p is a 971-amino-acid protein that is required for the nonsense-mediated mRNA decay (NMD) pathway, a pathway that degrades mRNAs with premature translational termination codons. We have identified a two-hybrid interaction between Upf1p and the nuclear pore (Nup) proteins, Nup100p and Nup116p. Both nucleoporins predominantly localize to the cytoplasmic side of the nuclear pore and participate in mRNA transport. The two-hybrid interaction between Upf1p and the nuclear pore proteins, Nup100p and Nup116p, is dependent on the presence of the C-terminal 158 amino acids of Upf1p. Nup100p and Nup116p can be co-immunoprecipitated from whole-cell extracts with Upf1p, confirming in vitro the interaction identified by the two-hybrid analysis. Finally, we see a genetic interaction between UPF1 and NUP100. The growth of upf1Δ, can1-100 cells is inhibited by canavanine. The deletion of NUP100 allows upf1Δ, can1-100 cells to grow in the presence of canavanine. Physiologically, the interaction between Upf1p and the nuclear pore proteins, Nup100p and Nup116p, is significant because it suggests a mechanism to ensure that Upf1p associates with newly synthesized mRNA as it is transported from the nucleus to the cytoplasm prior to the pioneer round of translation.
AB - Saccharomyces cerevisiae Upf1p is a 971-amino-acid protein that is required for the nonsense-mediated mRNA decay (NMD) pathway, a pathway that degrades mRNAs with premature translational termination codons. We have identified a two-hybrid interaction between Upf1p and the nuclear pore (Nup) proteins, Nup100p and Nup116p. Both nucleoporins predominantly localize to the cytoplasmic side of the nuclear pore and participate in mRNA transport. The two-hybrid interaction between Upf1p and the nuclear pore proteins, Nup100p and Nup116p, is dependent on the presence of the C-terminal 158 amino acids of Upf1p. Nup100p and Nup116p can be co-immunoprecipitated from whole-cell extracts with Upf1p, confirming in vitro the interaction identified by the two-hybrid analysis. Finally, we see a genetic interaction between UPF1 and NUP100. The growth of upf1Δ, can1-100 cells is inhibited by canavanine. The deletion of NUP100 allows upf1Δ, can1-100 cells to grow in the presence of canavanine. Physiologically, the interaction between Upf1p and the nuclear pore proteins, Nup100p and Nup116p, is significant because it suggests a mechanism to ensure that Upf1p associates with newly synthesized mRNA as it is transported from the nucleus to the cytoplasm prior to the pioneer round of translation.
KW - mRNA surveillance
KW - mRNA transport
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U2 - 10.1016/j.gene.2004.10.005
DO - 10.1016/j.gene.2004.10.005
M3 - Article
C2 - 15716093
AN - SCOPUS:13644266893
SN - 0378-1119
VL - 345
SP - 199
EP - 212
JO - Gene
JF - Gene
IS - 2
ER -