RRC ID |
67691
|
Author |
Aoyama K, Yuki R, Horiike Y, Kubota S, Yamaguchi N, Morii M, Ishibashi K, Nakayama Y, Kuga T, Hashimoto Y, Tomonaga T, Yamaguchi N.
|
Title |
Formation of long and winding nuclear F-actin bundles by nuclear c-Abl tyrosine kinase.
|
Journal |
Exp Cell Res
|
Abstract |
The non-receptor-type tyrosine kinase c-Abl is involved in actin dynamics in the cytoplasm. Having three nuclear localization signals (NLSs) and one nuclear export signal, c-Abl shuttles between the nucleus and the cytoplasm. Although monomeric actin and filamentous actin (F-actin) are present in the nucleus, little is known about the relationship between c-Abl and nuclear actin dynamics. Here, we show that nuclear-localized c-Abl induces nuclear F-actin formation. Adriamycin-induced DNA damage together with leptomycin B treatment accumulates c-Abl into the nucleus and increases the levels of nuclear F-actin. Treatment of c-Abl-knockdown cells with Adriamycin and leptomycin B barely increases the nuclear F-actin levels. Expression of nuclear-targeted c-Abl (NLS-c-Abl) increases the levels of nuclear F-actin even without Adriamycin, and the increased levels of nuclear F-actin are not inhibited by inactivation of Abl kinase activity. Intriguingly, expression of NLS-c-Abl induces the formation of long and winding bundles of F-actin within the nucleus in a c-Abl kinase activity-dependent manner. Furthermore, NLS-c-AblΔC, which lacks the actin-binding domain but has the full tyrosine kinase activity, is incapable of forming nuclear F-actin and in particular long and winding nuclear F-actin bundles. These results suggest that nuclear c-Abl plays critical roles in actin dynamics within the nucleus.
|
Volume |
319(20)
|
Pages |
3251-68
|
Published |
2013-12-10
|
DOI |
10.1016/j.yexcr.2013.09.003
|
PII |
S0014-4827(13)00385-6
|
PMID |
24041959
|
MeSH |
Actins / antagonists & inhibitors
Actins / biosynthesis*
Actins / chemistry
Animals
Binding Sites
COS Cells
Cell Nucleus / enzymology*
Cell Nucleus / metabolism
Chlorocebus aethiops
HeLa Cells
Humans
Mice
NIH 3T3 Cells
Phosphorylation
Proto-Oncogene Proteins c-abl / deficiency
Proto-Oncogene Proteins c-abl / metabolism*
Tyrosine / metabolism
|
IF |
3.383
|
Resource |
DNA material |
pENTR4-H1 (RDB04395) |