Abstract
Heat-shock protein 90 (Hsp90) is a molecular chaperone that plays a key role in the conformational maturation of various transcription factors and protein kinases in signal transduction. Multifunctional ribosomal protein S3 (rpS3), a component of the ribosomal small subunit, is involved in DNA repair and apoptosis. Our data show that Hsp90 binds directly to rpS3 and the functional consequence of Hsp90-rpS3 interaction results in the prevention of the ubiquitination and the proteasome-dependent degradation of rpS3, subsequently retaining the function and the biogenesis of the ribosome. Interference of Hsp90 activity by Hsp90 inhibitors appears to dissociate rpS3 from Hsp90, associate the protein with Hsp70, and induce the degradation of free forms of rpS3. Furthermore, ribosomal protein S6 (rpS6) also interacted with Hsp90 and exhibited a similar effect upon treatment with Hsp90 inhibitors. Therefore, we conclude that Hsp90 regulates the function of ribosomes by maintaining the stability of 40S ribosomal proteins such as rpS3 and rpS6.
| Original language | English |
|---|---|
| Pages (from-to) | 824-833 |
| Number of pages | 10 |
| Journal | Molecular Biology of the Cell |
| Volume | 17 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2006 Feb 1 |
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ASJC Scopus subject areas
- Molecular Biology
- Genetics
- Cell Biology
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Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation. / Kim, Tae Sung; Jang, Chang Young; Kim, Hag Dong; Lee, Jae Yung; Ahn, Byung-Yoon; Kim, Joon.
In: Molecular Biology of the Cell, Vol. 17, No. 2, 01.02.2006, p. 824-833.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation
AU - Kim, Tae Sung
AU - Jang, Chang Young
AU - Kim, Hag Dong
AU - Lee, Jae Yung
AU - Ahn, Byung-Yoon
AU - Kim, Joon
PY - 2006/2/1
Y1 - 2006/2/1
N2 - Heat-shock protein 90 (Hsp90) is a molecular chaperone that plays a key role in the conformational maturation of various transcription factors and protein kinases in signal transduction. Multifunctional ribosomal protein S3 (rpS3), a component of the ribosomal small subunit, is involved in DNA repair and apoptosis. Our data show that Hsp90 binds directly to rpS3 and the functional consequence of Hsp90-rpS3 interaction results in the prevention of the ubiquitination and the proteasome-dependent degradation of rpS3, subsequently retaining the function and the biogenesis of the ribosome. Interference of Hsp90 activity by Hsp90 inhibitors appears to dissociate rpS3 from Hsp90, associate the protein with Hsp70, and induce the degradation of free forms of rpS3. Furthermore, ribosomal protein S6 (rpS6) also interacted with Hsp90 and exhibited a similar effect upon treatment with Hsp90 inhibitors. Therefore, we conclude that Hsp90 regulates the function of ribosomes by maintaining the stability of 40S ribosomal proteins such as rpS3 and rpS6.
AB - Heat-shock protein 90 (Hsp90) is a molecular chaperone that plays a key role in the conformational maturation of various transcription factors and protein kinases in signal transduction. Multifunctional ribosomal protein S3 (rpS3), a component of the ribosomal small subunit, is involved in DNA repair and apoptosis. Our data show that Hsp90 binds directly to rpS3 and the functional consequence of Hsp90-rpS3 interaction results in the prevention of the ubiquitination and the proteasome-dependent degradation of rpS3, subsequently retaining the function and the biogenesis of the ribosome. Interference of Hsp90 activity by Hsp90 inhibitors appears to dissociate rpS3 from Hsp90, associate the protein with Hsp70, and induce the degradation of free forms of rpS3. Furthermore, ribosomal protein S6 (rpS6) also interacted with Hsp90 and exhibited a similar effect upon treatment with Hsp90 inhibitors. Therefore, we conclude that Hsp90 regulates the function of ribosomes by maintaining the stability of 40S ribosomal proteins such as rpS3 and rpS6.
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U2 - 10.1091/mbc.E05-08-0713
DO - 10.1091/mbc.E05-08-0713
M3 - Article
C2 - 16314389
AN - SCOPUS:31944445649
VL - 17
SP - 824
EP - 833
JO - Molecular Biology of the Cell
JF - Molecular Biology of the Cell
SN - 1059-1524
IS - 2
ER -