Disease relevance of ACTL6A

• Although it has a structure highly similar to ArpN beta/BAF53, ArpN alpha is expressed exclusively in brain and in neural differentiated embryonal carcinoma cells [1].

High impact information on ACTL6A

• BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-interacting nuclear cofactor for oncogenic transformation [2].
• When overexpressed in HeLa or 293T cells, the subdomain Ib or IIb hybrids, in which the subdomain Ib or IIb of hArpNbeta was replaced with that of beta-actin, respectively, showed no effect on cell survival [3].
• hArpNbeta, an actin-related protein located within the nucleus, is a subunit of the human SWI/SNF chromatin remodeling complex. hArpNbeta has been proposed to regulate the assembly and activity of the hSWI/SNF complex [3].
• These results indicate that the proper function of hArpNbeta is essential for cell survival in human cells [3].
• On the other hand, the overexpression of the N-terminal deletion mutant of hArpNbeta resulted in cell death probably through apoptotic process [3].

Biological context of ACTL6A

• Generation of the dominant-negative mutant of hArpNbeta: a component of human SWI/SNF chromatin remodeling complex [3].
• Since the proposed function of hArpNbeta requires more than two distinct but concurrently operating surfaces, we examined whether the disruption of one operating surface of hArpNbeta results in dominant-negative phenotype [3].
• We identified two alternative splicing products of the gene for hArpNbeta/ Baf53 [4].
• Effects of Ser2 and Tyr6 mutants of BAF53 on cell growth and p53-dependent transcription [5].

Anatomical context of ACTL6A

• Previously we showed that over-expression of an N-terminal deletion mutant of BAF53 (BAF53_deltaN) reduced the viability of HEK293 and HeLa cells [5].

Associations of ACTL6A with chemical compounds

• Our results demonstrate that serine 2 and tyrosine 6 play important roles in BAF53 activity [5].
• When we replaced the serine 2 and tyrosine 6 of this N-terminal motif with alanine, over-expression of the alanine-replaced BAF53 strongly impaired the growth of HEK293 cells whereas replacement with aspartate/glutamate had no effect [5].
• Shuttling was not blocked by leptomycin B, indicating that export of BAF53 is not mediated by CRM1 [6].

Other interactions of ACTL6A

• We identified mouse ArpNalpha, and showed that ArpNalpha is more similar between humans and mice than ArpNbeta [7].
• BAF53 (also known as ArpNbeta) is a nuclear arp that is a component of a number of chromatin-modifying complexes, such as the SWI/SNF and TRRAP complexes [6].
• A human nuclear actin-related protein, hArpNbeta/ Baf53, is a component of chromatin remodeling and histone acetyltransferase complexes [4].

References