Unknown

Dataset Information

0

Actin-related proteins localized in the nucleus: from discovery to novel roles in nuclear organization.


ABSTRACT: The actin family consists of conventional actin and actin-related proteins (ARPs), and the members show moderate similarity and share the same basal structure. Following the finding of various ARPs in the cytoplasm in the 1990s, multiple subfamilies that are localized predominantly in the nucleus were identified. Consistent with these cytological observations, subsequent biochemical analyses revealed the involvement of the nuclear ARPs in ATP-dependent chromatin-remodeling and histone acetyltransferase complexes. In addition to their contribution to chromatin remodeling, recent studies have shown that nuclear ARPs have roles in the organization of the nucleus that are independent of the activity of the above-mentioned complexes. Therefore, nuclear ARPs are recognized as novel key regulators of genome function, and affect not only the remodeling of chromatin but also the spatial arrangement and dynamics of chromatin within the nucleus.

SUBMITTER: Oma Y 

PROVIDER: S-EPMC3104808 | biostudies-literature | 2011 Jan-Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Actin-related proteins localized in the nucleus: from discovery to novel roles in nuclear organization.

Oma Yukako Y   Harata Masahiko M  

Nucleus (Austin, Tex.) 20110101 1


The actin family consists of conventional actin and actin-related proteins (ARPs), and the members show moderate similarity and share the same basal structure. Following the finding of various ARPs in the cytoplasm in the 1990s, multiple subfamilies that are localized predominantly in the nucleus were identified. Consistent with these cytological observations, subsequent biochemical analyses revealed the involvement of the nuclear ARPs in ATP-dependent chromatin-remodeling and histone acetyltran  ...[more]

Similar Datasets

| S-EPMC3210522 | biostudies-literature
| S-EPMC2800988 | biostudies-literature
| S-EPMC8070096 | biostudies-literature
| S-EPMC3117639 | biostudies-literature
| S-EPMC2810487 | biostudies-literature
| S-EPMC5057282 | biostudies-literature
| PRJEB17838 | ENA
| S-EPMC5445336 | biostudies-literature
| S-EPMC4231706 | biostudies-literature
| S-EPMC5053997 | biostudies-literature