Cytochemical Localization of Actin and Myosin Aggregates in Interphase Nuclei in Situ

Milankov, K.; Boni, U. De

doi:10.1006/excr.1993.1301

Cited by 67 publications

(39 citation statements)

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“…However, actin can also form a multitude of special dimers, short protofilaments and tubular, flat or branched oligomers that would suit the chromatin-dominated nuclear space (Pederson and Aebi, 2002). Interestingly, nuclear actin polymers adopt a unique conformation that is recognized by specific antibodies (Milankov and De Boni, 1993). Actin binds directly to two regions in the lamin A/C tail: residues 461-536 (in the Ig-fold domain) (M.S.Z.…”

Section: Architectural Partnersmentioning

confidence: 99%

Proteins that bind A-type lamins: integrating isolated clues

Zastrow

Vlcek

Wilson

2004

Journal of Cell Science

202

189

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What do such diverse molecules as DNA, actin, retinoblastoma protein and protein kinase Cα all have in common? They and additional partners bind `A-type' lamins, which form stable filaments in animal cell nuclei. Mutations in A-type lamins cause a bewildering range of tissue-specific diseases, termed `laminopathies', including Emery-Dreifuss muscular dystrophy and the devastating Hutchinson-Gilford progeria syndrome, which mimics premature aging. Considered individually and collectively, partners for A-type lamins form four loose groups: architectural partners, chromatin partners, gene-regulatory partners and signaling partners. We describe 16 partners in detail, summarize their binding sites in A-type lamins, and sketch portraits of ternary complexes and functional pathways that might depend on lamins in vivo. On the basis of our limited current knowledge, we propose lamin-associated complexes with multiple components relevant to nuclear structure (e.g. emerin, nesprin 1α, actin) or signaling and gene regulation (e.g. LAP2α, retinoblastoma, E2F-DP heterodimers, genes) as `food for thought'. Testing these ideas will deepen our understanding of nuclear function and human disease.

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Section: Architectural Partnersmentioning

confidence: 99%

Proteins that bind A-type lamins: integrating isolated clues

Zastrow

Vlcek

Wilson

2004

Journal of Cell Science

202

189

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“…In our previous studies, we showed actin's presence in the nuclei of different cell lines treated with various cytostatic drugs including DOX (6,24). There are reports on the existence of actin in interphase nuclei (25,26). It is assumed that nuclear actin binds some structural proteins within the nucleus (27).…”

Section: Introductionmentioning

confidence: 95%

Actin reorganization in CHO AA8 cells undergoing mitotic catastrophe and apoptosis induced by doxorubicin

Grzanka¹

2010

Oncol Rep

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Abstract. Doxorubicin (DOX) is a drug widely used in cancer chemotherapy. Although it has been proven that DOX kills tumor cells, the triggered modes of cell death are not fully understood. There is some evidence that, depending on the dose of DOX, the treated cells undergo senescence, mitotic catastrophe, apoptosis or necrosis. The aim of this study was to assess the type of CHO AA8 cell death induced with different DOX doses. In this context, we also assessed organization and distribution of F-actin, which integrity was suggested to be indispensable for apoptosis. Following treatment with 0.5 and 1 μM DOX, the giant multinucleated cells with extended network of fine microfilaments appeared. Notably, in the nuclei of the enlarged cells microscopy and cytometric analysis showed the presence of F-actin. DOX (2.5 μM) caused the appearance of the giant cells and with apoptotic features and signs of autophagy vacuolization. Flow cytometric studies indicated a dose-dependent increase in the number of TUNELpositive cells and cells stained with both Annexin V and PI. Cell cycle analysis revealed the increase in the hyperploid DNA content. Our results suggest that treatment of CHO AA8 cells with different DOX doses caused mitotic catastrophe that was followed by apoptosis with signs of autophagy. The increase in F-actin content in the nuclei of the dying cells was evident. We hypothesize that in CHO AA8 cells F-actin may be involved in chromatin reorganization undergoing cell death.

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“…An association of actin with various chromatin states has been shown by a number of studies (Milankov and De, 1993;Sauman and Berry, 1994). Bacterial actin was shown to be involved in plasmid and chromosome segregation (Becker et al, 2006;Moller-Jensen et al, 2007).…”

Section: Roles Of Actin In Genome Organizationmentioning

confidence: 88%