Details
| Original language | English |
|---|---|
| Pages (from-to) | 93-100 |
| Number of pages | 8 |
| Journal | Molecular and Cellular Biochemistry |
| Volume | 307 |
| Issue number | 1-2 |
| Publication status | Published - Jan 2008 |
Abstract
Importin 13 is a member of the importin β superfamily of nuclear transport proteins and is expressed in multiple tissues at high levels both in humans and rodents, including fetal lung, brain, and heart. In order to elucidate potential functions of imp13 in the heart, we have used rat imp13 as bait to screen a human heart cDNA library and identified an interaction with the C-terminal peptide of myopodin (a.a. 360-698), an actin-bundling protein, associated with tumor-suppressor activity that localizes to both the cytoplasm and the nucleus. We have used GST-pull down assays and co-immunoprecipitation experiments to demonstrate an interaction between imp13 and full-length myopodin and observed that RanGTP dissociates the myopodin-imp13 complex. In studies of cultured cells, we show that both imp13 siRNA and a C-terminal fragment of imp13 protein prevent nuclear localization of myopodin. We, therefore, conclude that imp13 functions in myopodin import and we suggest that the regulation of these events is critical for normal and abnormal cellular differentiation.
Keywords
- Importin 13, Interaction, Myopodin, Nuclear import
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Clinical Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: Molecular and Cellular Biochemistry, Vol. 307, No. 1-2, 01.2008, p. 93-100.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Interaction between importin 13 and myopodin suggests a nuclear import pathway for myopodin
AU - Liang, Jie
AU - Ke, Guifen
AU - You, Wenjun
AU - Peng, Zi
AU - Lan, Jie
AU - Kalesse, Markus
AU - Tartakoff, Alan M.
AU - Kaplan, Feige
AU - Tao, Tao
N1 - Funding Information: Acknowledgments This work was supported by grants (#3047085 and #90608007 from the National Natural Science Foundation of China; #C0510003 from the Natural Science Foundation of Fujian Province; #2005-383 from the Ministry of Education of China) and a startup fund (#XK0014) from Xiamen University to Tao Tao.
PY - 2008/1
Y1 - 2008/1
N2 - Importin 13 is a member of the importin β superfamily of nuclear transport proteins and is expressed in multiple tissues at high levels both in humans and rodents, including fetal lung, brain, and heart. In order to elucidate potential functions of imp13 in the heart, we have used rat imp13 as bait to screen a human heart cDNA library and identified an interaction with the C-terminal peptide of myopodin (a.a. 360-698), an actin-bundling protein, associated with tumor-suppressor activity that localizes to both the cytoplasm and the nucleus. We have used GST-pull down assays and co-immunoprecipitation experiments to demonstrate an interaction between imp13 and full-length myopodin and observed that RanGTP dissociates the myopodin-imp13 complex. In studies of cultured cells, we show that both imp13 siRNA and a C-terminal fragment of imp13 protein prevent nuclear localization of myopodin. We, therefore, conclude that imp13 functions in myopodin import and we suggest that the regulation of these events is critical for normal and abnormal cellular differentiation.
AB - Importin 13 is a member of the importin β superfamily of nuclear transport proteins and is expressed in multiple tissues at high levels both in humans and rodents, including fetal lung, brain, and heart. In order to elucidate potential functions of imp13 in the heart, we have used rat imp13 as bait to screen a human heart cDNA library and identified an interaction with the C-terminal peptide of myopodin (a.a. 360-698), an actin-bundling protein, associated with tumor-suppressor activity that localizes to both the cytoplasm and the nucleus. We have used GST-pull down assays and co-immunoprecipitation experiments to demonstrate an interaction between imp13 and full-length myopodin and observed that RanGTP dissociates the myopodin-imp13 complex. In studies of cultured cells, we show that both imp13 siRNA and a C-terminal fragment of imp13 protein prevent nuclear localization of myopodin. We, therefore, conclude that imp13 functions in myopodin import and we suggest that the regulation of these events is critical for normal and abnormal cellular differentiation.
KW - Importin 13
KW - Interaction
KW - Myopodin
KW - Nuclear import
UR - http://www.scopus.com/inward/record.url?scp=36949022695&partnerID=8YFLogxK
U2 - 10.1007/s11010-007-9588-1
DO - 10.1007/s11010-007-9588-1
M3 - Article
C2 - 17828378
AN - SCOPUS:36949022695
VL - 307
SP - 93
EP - 100
JO - Molecular and Cellular Biochemistry
JF - Molecular and Cellular Biochemistry
SN - 0300-8177
IS - 1-2
ER -