Abstract
The mammalian cytoskeletal proteins β- and γ-actin are highly homologous, but only β-actin is amino-terminally arginylated in vivo, which regulates its function. We examined the metabolic fate of exogenously expressed arginylated and nonarginylated actin isoforms. Arginylated γ-actin, unlike β-, was highly unstable and was selectively ubiquitinated and degraded in vivo. This instability was regulated by the differences in the nucleotide coding sequence between the two actin isoforms, which conferred different translation rates. γ-actin was translated more slowly than β-actin, and this slower processing resulted in the exposure of a normally hidden lysine residue for ubiquitination, leading to the preferential degradation of γ-actin upon arginylation. This degradation mechanism, coupled to nucleotide coding sequence, may regulate protein arginylation in vivo.
| Original language | English |
|---|---|
| Pages (from-to) | 1534-1537 |
| Number of pages | 4 |
| Journal | Science |
| Volume | 329 |
| Issue number | 5998 |
| DOIs | |
| State | Published - Sep 17 2010 |
| Externally published | Yes |
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Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation. / Zhang, Fangliang; Saha, Sougata; Shabalina, Svetlana A.; Kashina, Anna.
In: Science, Vol. 329, No. 5998, 17.09.2010, p. 1534-1537.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation
AU - Zhang, Fangliang
AU - Saha, Sougata
AU - Shabalina, Svetlana A.
AU - Kashina, Anna
PY - 2010/9/17
Y1 - 2010/9/17
N2 - The mammalian cytoskeletal proteins β- and γ-actin are highly homologous, but only β-actin is amino-terminally arginylated in vivo, which regulates its function. We examined the metabolic fate of exogenously expressed arginylated and nonarginylated actin isoforms. Arginylated γ-actin, unlike β-, was highly unstable and was selectively ubiquitinated and degraded in vivo. This instability was regulated by the differences in the nucleotide coding sequence between the two actin isoforms, which conferred different translation rates. γ-actin was translated more slowly than β-actin, and this slower processing resulted in the exposure of a normally hidden lysine residue for ubiquitination, leading to the preferential degradation of γ-actin upon arginylation. This degradation mechanism, coupled to nucleotide coding sequence, may regulate protein arginylation in vivo.
AB - The mammalian cytoskeletal proteins β- and γ-actin are highly homologous, but only β-actin is amino-terminally arginylated in vivo, which regulates its function. We examined the metabolic fate of exogenously expressed arginylated and nonarginylated actin isoforms. Arginylated γ-actin, unlike β-, was highly unstable and was selectively ubiquitinated and degraded in vivo. This instability was regulated by the differences in the nucleotide coding sequence between the two actin isoforms, which conferred different translation rates. γ-actin was translated more slowly than β-actin, and this slower processing resulted in the exposure of a normally hidden lysine residue for ubiquitination, leading to the preferential degradation of γ-actin upon arginylation. This degradation mechanism, coupled to nucleotide coding sequence, may regulate protein arginylation in vivo.
UR - http://www.scopus.com/inward/record.url?scp=77956663124&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77956663124&partnerID=8YFLogxK
U2 - 10.1126/science.1191701
DO - 10.1126/science.1191701
M3 - Article
C2 - 20847274
AN - SCOPUS:77956663124
VL - 329
SP - 1534
EP - 1537
JO - Science
JF - Science
SN - 0036-8075
IS - 5998
ER -