The Drosophila fs(1)Ya Protein, Which Is Needed for the First Mitotic Division, Is in the Nuclear Lamina and in the Envelopes of Cleavage Nuclei, Pronuclei, and Nonmitotic Nuclei

Lopez, Jacqueline M.; Song, Kiwon; Hirshfeld, A.B.; Lin, Haifan; Wolfner, Mariana F.

doi:10.1006/dbio.1994.1136

Cited by 30 publications

(39 citation statements)

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“…We transfected GFP-NLS-YA constructs into Drosophila S2 cells. These cells correctly target wild-type YA expressed during transient transfection [data not shown; expressed YA is seen in the nucleoplasm and nuclear periphery, as previously reported for wild-type YA transiently transfected into Drosophila Kc cells (Lopez et al, 1994)]. S2 cells do not contain endogenous YA (data not shown) that compete with the expressed fusion protein for binding with endogenous molecular partners.…”

Section: Resultssupporting

confidence: 65%

“…Although these GFP-NLS-YA fusions are targeted to the nuclear periphery, there is also nucleoplasmic staining. Because this distribution is like that seen with full-length YA expressed in Kc cells (Lopez et al, 1994), we believe that it reflects binding of YA sequences to a minor population of lamin Dm0 found by P. Fisher and colleagues to reside in the interior of the Drosophila nucleus (P. Fisher, personal communication) or to chromatin (Yu and Wolfner, 2002) or saturation of YA binding sites owing to high level expression of the transfected DNA. Lamin-GFP fusions have also been reported to localize to the interior of the nucleus (in addition to the nuclear periphery) in transfected mammalian cells (Broers et al, 1999).…”

Section: Subcellular Localization Of Gfp-nls-ya Deletions In Transfecsupporting

confidence: 62%

“…These results show that the Cterminal region of YA (residues 506-696), the region that interacts with lamin Dm0 in the yeast two-hybrid system, is sufficient to target a heterologous protein to the Drosophila nuclear periphery. The location of the GFP-NLS-YA fusion in transfected S2 cells was nearly identical to that of wild-type (untagged) YA expressed in transfected Kc cells (Lopez et al, 1994). Interestingly, preliminary experiments using mammalian HEK cells (S.S.M., unpublished) suggest that the same YA domain fused to GFP-NLS is not sufficient to target the reporter protein to the mammalian nuclear periphery.…”

Section: Resultsmentioning

confidence: 88%

“…Lamin Dm0 is present in the nuclei of all cells in which YA is in the nuclear envelope Liu et al, 1995;Lopez et al, 1994). At metaphase, the two proteins disappear from the nuclear periphery simultaneously, as one would expect if the presence of YA at the nuclear periphery depended on the presence of polymerized lamin.…”

Section: Subcellular Localization Of Gfp-nls-ya Deletions In Transfecmentioning

confidence: 93%

“…When the lamin-interaction region of YA is deleted, YA still enters nuclei but fails to localize to nuclear envelopes, suggesting that lamin interaction targets YA to the nuclear envelope. Here, we show that C-terminal lamin-interacting region of YA is sufficient to target the heterologous soluble protein GFP-NLS to the nuclear periphery in Lopez et al, 1994). This entirely hydrophilic protein, with no discernible lipid modification or membrane-targeting motifs, is required for fertilized eggs to enter the mitotic cleavage phase of early development.…”

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confidence: 94%

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A hydrophilic lamin-binding domain from theDrosophilaYA protein can target proteins to the nuclear envelope

Mani

Rajagopal

Garfinkel

et al. 2003

Journal of Cell Science

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The nuclear lamina provides an architectural framework for the nuclear envelope and an attachment site for interphase chromatin. In Drosophila eggs and early embryos its major constituent, lamin Dm0, interacts with a lamina protein called YA. When the lamin-interaction region of YA is deleted, YA still enters nuclei but fails to localize to nuclear envelopes, suggesting that lamin interaction targets YA to the nuclear envelope. Here, we show that C-terminal lamin-interacting region of YA is sufficient to target the heterologous soluble protein GFP-NLS to the nuclear periphery in Drosophila tissue culture cells. Yeast two-hybrid analysis and transient transfection assays further defined this domain: residues 556-696 of YA are sufficient for both lamin Dm0interaction and the targeting of GFP-NLS to the nuclear periphery. This region of YA is hydrophilic and lacks any transmembrane domain or known membrane-targeting motifs. We propose that the localization of YA to the nuclear lamina involves interaction with polymerized lamin Dm0mediated by the lamin-targeting domain of YA. This hydrophilic YA domain might provide a useful molecular tool for targeting heterologous non-membrane-associated proteins to the nuclear envelope.

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Section: Resultssupporting

confidence: 65%

Section: Subcellular Localization Of Gfp-nls-ya Deletions In Transfecsupporting

confidence: 62%

Section: Resultsmentioning

confidence: 88%

Section: Subcellular Localization Of Gfp-nls-ya Deletions In Transfecmentioning

confidence: 93%

mentioning

confidence: 94%

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A hydrophilic lamin-binding domain from theDrosophilaYA protein can target proteins to the nuclear envelope

Mani

Rajagopal

Garfinkel

et al. 2003

Journal of Cell Science

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Formation of the Male Pronuclear Lamina inDrosophila melanogaster

Lin

Lopez

et al. 1997

Developmental Biology

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Upon fertilization, a sperm nucleus reorganizes to become a male pronucleus. This reorganization includes breakdown and reformation of the nuclear envelope of the male pronucleus. In this study, we used a maternally encoded nuclear lamina protein, YA, in parallel with another lamina protein, lamin Dm, as probes to study the formation of the male pronuclear lamina in Drosophila melanogaster. Ectopically expressed YA is present in the nuclear envelopes of spermatocytes, but not in mature sperm, similar to endogenous lamin Dm. This suggests that the nuclear envelope of Drosophila sperm differs from that of somatic cells. Upon fertilization, YA and lamin Dm are recruited to the periphery of the male-derived nucleus before or during the early stages of migration by the male pronucleus. Using a paternal effect mutation, snky, we found that recruitment of lamina proteins to the male pronucleus requires, and probably accompanies, reorganization of the sperm nucleus. In order to identify factors that affect the recruitment of nuclear lamina proteins to the male pronucleus, we examined the subcellular localization of YA and lamin Dm in mutant embryos defective for the function of either the male pronucleus (mh, K81, and pal or both pronuclei (gnu, png, and plu). None of these mutations affect the recruitment of YA or lamin Dm to the male pronuclear envelope, suggesting that the mutations affect processes independent of, or after, reorganization of the nuclear envelope. Double mutant analyses between Ya and gnu suggest that YA plays a role in the nuclear envelope permissive for rounds of DNA replication.

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Nuclear Entry of theDrosophila melanogasterNuclear Lamina Protein YA Correlates with Developmentally Regulated Changes in Its Phosphorylation State

Song

Turner

et al. 1999

Developmental Biology

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The Drosophila melanogaster YA protein is a maternally provided nuclear lamina component that is essential during the transition from meiosis to mitosis at the beginning of embryogenesis. Localization of YA to the nuclear envelope is required for its function; this localization is cell cycle-dependent during embryogenesis. Here we show that the ability of YA to enter nuclei is modulated during development. In developing egg chambers, YA protein is made but excluded from nuclei of nurse cells and oocytes; upon egg activation, YA acquires the ability to enter nuclei and becomes incorporated into the nuclear lamina in unfertilized eggs and embryos. This localization switch correlates with changes in the phosphorylation state of YA. YA in ovaries is hyperphosphorylated relative to YA in unfertilized eggs and embryos. Through site-directed mutagenesis, we identified 443T, a potential phosphorylation site for both cyclin-dependent protein kinase and mitogen-activated-protein kinase, as one of the sites likely involved in this developmental control. Our results suggest that phosphorylation plays a role in modulating the localization of YA during development. A model for developmental regulation of the nuclear entry of YA is proposed and implications for understanding Drosophila egg activation are discussed.

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The Drosophila fs(1)Ya Protein, Which Is Needed for the First Mitotic Division, Is in the Nuclear Lamina and in the Envelopes of Cleavage Nuclei, Pronuclei, and Nonmitotic Nuclei

Cited by 30 publications

References 0 publications

A hydrophilic lamin-binding domain from theDrosophilaYA protein can target proteins to the nuclear envelope

A hydrophilic lamin-binding domain from theDrosophilaYA protein can target proteins to the nuclear envelope

Formation of the Male Pronuclear Lamina inDrosophila melanogaster

Nuclear Entry of theDrosophila melanogasterNuclear Lamina Protein YA Correlates with Developmentally Regulated Changes in Its Phosphorylation State

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