Extraktion eines dem Aktin ähnlichen Proteins aus dem Zellkern des Kalbsthymus

Ohnishi, Tsuyoshi; Kawamura, Hiroé; Yamamoto, Tamio

doi:10.1093/oxfordjournals.jbchem.a127789

Cited by 34 publications

(7 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It has been shown to be important for cytokinesis and cell shape changes during cell division. In dictyostelium, null mutants of NMHC II are multinucleate, lack contractile The localization of nonmuscle myosin in the nucleus has been speculated by other workers since the pioneering work of Ohnishi et al (1963) and later by Jockusch et al (1970Jockusch et al ( , 1971. Lestourgeon et al (1975) also demonstrated that nonmuscle myosin is a component of the nuclei in both HeLa S3 and in mouse embryo fibroblasts, the two cell lines that we have used in our study.…”

Section: Discussionsupporting

confidence: 55%

Menin, a tumor suppressor, associates with nonmuscle myosin II-A heavy chain

et al. 2003

View full text Add to dashboard Cite

MEN1 is a likely tumor suppressor gene that encodes a novel protein, menin. Menin is a 610 amino-acid residue protein with as yet unknown function(s). We have used tandem affinity purification and mass spectroscopy to isolate and identify proteins associating with menin from cultured HeLa cell extracts. This strategy has resulted in the isolation and identification of nonmuscle myosin type II-A heavy chain (NMHC II-A) as a menin interacting protein. This interaction was confirmed by glutathione-Stransferase pulldown assays, by coimmunoprecipitation, and by actin selection of myosin. We have further identified the amino-terminal region of menin and the head domain of NMHC II-A to be regions required for this interaction. Moreover menin was seen to colocalize with this myosin isoform in the cleavage furrow of dividing cells by indirect immunofluoresence. These data indicate that menin through binding to NMHC II-A could participate in cell division and in other processes that involve NMHC II-A.

show abstract

Section: Discussionsupporting

confidence: 55%

Menin, a tumor suppressor, associates with nonmuscle myosin II-A heavy chain

et al. 2003

View full text Add to dashboard Cite

show abstract

“…The original studies were largely observational. The first ones described actin in the nuclear subcellular fraction of calf thymus cells (Ohnishi et al, 1963; Ohnishi et al, 1964). Soon after, nuclear actin was described by Nancy Lane (1969), who initially demonstrated using electron microscopy that fibrillar bodies form in the nucleoplasm of Triturus viridescens (newt) oocytes in response to actinomycin D treatment, which inhibits global transcription.…”

Section: Early Observations Of Actin In the Nucleusmentioning

confidence: 99%

Nuclear Actin: From Discovery to Function

Kelpsch

Tootle

2018

The Anatomical Record

View full text Add to dashboard Cite

While actin was discovered in the nucleus over 50 years ago, research lagged for decades due to strong skepticism. The revitalization of research into nuclear actin occurred after it was found that cellular stresses induce the nuclear localization and alter the structure of actin. These studies provided the first hints that actin has a nuclear function. Subsequently, it was established that the nuclear import and export of actin is highly regulated. While the structures of nuclear actin remain unclear, it can function as monomers, polymers, and even rods. Furthermore, even within a given structure, distinct pools of nuclear actin that can be differentially labeled have been identified. Numerous mechanistic studies have uncovered an array of functions for nuclear actin. It regulates the activity of RNA polymerases, as well as specific transcription factors. Actin also modulates the activity of several chromatin remodeling complexes and histone deacetylases, to ultimately impinge on transcriptional programing and DNA damage repair. Further, nuclear actin mediates chromatin movement and organization. It has roles in meiosis and mitosis, and these functions may be functionally conserved from ancient bacterial actin homologs. The structure and integrity of the nuclear envelope and sub-nuclear compartments are also regulated by nuclear actin. Furthermore, nuclear actin contributes to human diseases like cancer, neurodegeneration, and myopathies. Here, we explore the early discovery of actin in the nucleus and discuss the forms and functions of nuclear actin in both normal and disease contexts

show abstract

“…In addition to its well-established cytoskeletal roles, actin also localizes to and functions within the nucleus. Nuclear actin was first reported over 50 years ago (Ohnishi et al , 1963; Ohnishi et al , 1964; Lane, 1969). These finding were met with skepticism.…”

Section: Introductionmentioning

confidence: 99%

Multiple Pools of Nuclear Actin

Wineland

Kelpsch

Tootle

2018

The Anatomical Record

View full text Add to dashboard Cite

While nuclear actin was reported ~50 years ago, it’s in vivo prevalence and structure remain largely unknown. Here we use Drosophila oogenesis, i.e. follicle development, to characterize nuclear actin. We find that three different reagents – DNase I, anti-actin C4, and anti-actin AC15 – recognize distinct pools of nuclear actin. DNase I labels monomeric or G-actin, and, during follicle development, G-actin is present in the nucleus of every cell. Some G-actin is recognized by the C4 antibody. In particular, C4 nuclear actin colocalizes with DNase I to the nucleolus in anterior escort cells, follicle stem cells, some mitotic follicle cells, and a subset of nurse cells during early oogenesis. C4 also labels polymeric nuclear actin in the nucleoplasm of the germline stem cells, early cystoblasts, and oocytes. The AC15 antibody labels a completely distinct pool of nuclear actin from that of DNase I and C4. Specifically, AC15 nuclear actin localizes to the chromatin in the nurse and follicle cells during mid-to-late oogenesis. Within the oocyte, AC15 nuclear actin progresses from localizing to puncta surrounding the DNA, to forming a filamentous cage around the chromosomes. Together these findings reveal that nuclear actin is highly prevalent in vivo, and multiple pools of nuclear actin exist and can be recognized using different reagents. Additionally, our localization studies suggest that nuclear actin may regulate stemness, nucleolar structure and function, transcription, and nuclear structure. Such findings call for further studies to explore the prevalence, diversity, and functions of nuclear actin across tissues and organisms.

show abstract

Extraktion eines dem Aktin ähnlichen Proteins aus dem Zellkern des Kalbsthymus

Cited by 34 publications

References 0 publications

Menin, a tumor suppressor, associates with nonmuscle myosin II-A heavy chain

Menin, a tumor suppressor, associates with nonmuscle myosin II-A heavy chain

Nuclear Actin: From Discovery to Function

Multiple Pools of Nuclear Actin

Contact Info

Product

Resources

About