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

Oma, Yukako; Harata, Masahiko

doi:10.4161/nucl.2.1.14510

Cited by 40 publications

(24 citation statements)

References 119 publications

(144 reference statements)

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“…However, the nuclear localisation of other ARP proteins has been described, initially in budding yeast and, more recently, in vertebrates (reviewed by Oma and Harata, 2011). Specifically ARP4, ARP5, ARP6 and ARP8 localise to the nucleus in vertebrates (Harata et al, 1999;Kato et al, 2001;Ohfuchi et al, 2006;Aoyama et al, 2008;Kitayama et al, 2009) and ARP4 and ARP5 have been shown to shuttle between the nucleus and the cytoplasm in human cell lines Kitayama et al, 2009).…”

Section: Nuclear Arp Proteinsmentioning

confidence: 99%

“…Specifically ARP4, ARP5, ARP6 and ARP8 localise to the nucleus in vertebrates (Harata et al, 1999;Kato et al, 2001;Ohfuchi et al, 2006;Aoyama et al, 2008;Kitayama et al, 2009) and ARP4 and ARP5 have been shown to shuttle between the nucleus and the cytoplasm in human cell lines Kitayama et al, 2009). The nuclear ARP proteins, along with actin, are components of large chromatin-modifying complexes, including nucleosome remodelling and certain histone acetyltransferase (HAT) complexes, and are involved in multiple nuclear functions including transcription, DNA repair and replication, and chromosome segregation (reviewed in Oma and Harata, 2011). For example, ARP4, ARP5 and ARP8, together with actin, form subunits of the mammalian INO80 chromatin-remodelling complex that functions in transcriptional regulation, DNAdamage-induced double strand break repair and the nucleotide excision repair (NER) pathway (Jin et al, 2005;Jiang et al, 2010).…”

Section: Nuclear Arp Proteinsmentioning

confidence: 99%

See 1 more Smart Citation

Actin nucleators in the nucleus: an emerging theme

Weston

Coutts

Thangué

2012

Journal of Cell Science

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SummaryActin is an integral component of the cytoskeleton, forming a plethora of macromolecular structures that mediate various cellular functions. The formation of such structures relies on the ability of actin monomers to associate into polymers, and this process is regulated by actin nucleation factors. These factors use monomeric actin pools at specific cellular locations, thereby permitting rapid actin filament formation when required. It has now been established that actin is also present in the nucleus, where it is implicated in chromatin remodelling and the regulation of eukaryotic gene transcription. Notably, the presence of typical actin filaments in the nucleus has not been demonstrated directly. However, studies in recent years have provided evidence for the nuclear localisation of actin nucleation factors that promote cytoplasmic actin polymerisation. Their localisation to the nucleus suggests that these proteins mediate collaboration between the cytoskeleton and the nucleus, which might be dependent on their ability to promote actin polymerisation. The nature of this cooperation remains enigmatic and it will be important to elucidate the physiological relevance of the link between cytoskeletal actin networks and nuclear events. This Commentary explores the current evidence for the nuclear roles of actin nucleation factors. Furthermore, the implication of actin-associated proteins in relaying exogenous signals to the nucleus, particularly in response to cellular stress, will be considered.

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Section: Nuclear Arp Proteinsmentioning

confidence: 99%

Section: Nuclear Arp Proteinsmentioning

confidence: 99%

Actin nucleators in the nucleus: an emerging theme

Weston

Coutts

Thangué

2012

Journal of Cell Science

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“…After many years of controversy, it is now accepted that the nucleus contains abundant G-actin, although F-actin has not been detected (Gettemans et al 2005, Pederson 2008, Zheng et al 2009, Visa & Percipalle 2010, de Lanerolle & Serebryannyy 2011, Oma & Harata 2011. However, a number of F-actin-binding proteins are found in nuclei.…”

Section: Introductionmentioning

confidence: 99%

Actin dynamics regulate subcellular localization of the F-actin-binding protein PALLD in mouse Sertoli cells

Niedenberger¹,

Chappell²,

Otey³

et al. 2014

Reproduction

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Sertoli cells undergo terminal differentiation at puberty to support all phases of germ cell development, which occurs in the mouse beginning in the second week of life. By w18 days postpartum (dpp), nearly all Sertoli cells have ceased proliferation. This terminal differentiation is accompanied by the development of unique and regionally concentrated filamentous actin (F-actin) structures at the basal and apical aspects of the seminiferous epithelium, and this reorganization is likely to involve the action of actin-binding proteins. Palladin (PALLD) is a widely expressed F-actin-binding and bundling protein recently shown to regulate these structures, yet it is predominantly nuclear in Sertoli cells at puberty. We found that PALLD localized within nuclei of primary Sertoli cells grown in serumfree media but relocalized to the cytoplasm upon serum stimulation. We utilized this system with in vivo relevance to Sertoli cell development to investigate mechanisms regulating nuclear localization of this F-actin-binding protein. Our results indicate that PALLD can be shuttled from the nucleus to the cytoplasm, and that this relocalization occurred following depolymerization of the F-actin cytoskeleton in response to cAMP signaling. Nuclear localization was reduced in Hpg-mutant testes, suggesting the involvement of gonadotropin signaling. We found that PALLD nuclear localization was unaffected in testis tissues from LH receptor and androgen receptor-mutant mice. However, PALLD nuclear localization was reduced in the testes of FSH receptor-mutant mice, suggesting that FSH signaling during Sertoli cell maturation regulates this subcellular localization.

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“…cTnT is a protein whose only known function is as part of the troponin complex of myofibrils in cardiac and embryonic skeletal muscles (Antin et al 2002). Alpha-actin is one of the isoforms of the actin family found in muscle tissue (Oma and Harata 2011). Gap junctions play significant regulatory roles in embryonic development, electrical coupling, metabolic transport, apoptosis, differentiation, tissue homeostasis and carcinogenesis (Laird 2010).…”

Section: Cultured Afs Cells (Both C-kitmentioning

confidence: 99%