Role of Adducin-like (hu-li tai shao) mRNA and protein localization in regulating cytoskeletal structure and function during Drosophila Oogenesis and early embryogenesis.

  title={Role of Adducin-like (hu-li tai shao) mRNA and protein localization in regulating cytoskeletal structure and function during Drosophila Oogenesis and early embryogenesis.},
  author={Mary Zaccai and Howard D. Lipshitz},
  journal={Developmental genetics},
  volume={19 3},
Adducin is a cytoskeletal protein that can function in vitro to bundle F-actin and to control the assembly of the F-actin/spectrin cytoskeletal network. We previously reported cloning of the Drosophila Adducin-like (Add) locus [Ding et al., 1993] also referred to as hu-li tai shao (hts) [Yue and Spradling, 1992], and identification of two adducin-related protein isoforms: a 95 x 10(3) Mr form (ADD-95) and an 87 x 10(3) Mr form (ADD-87) [Zaccai and Lipshitz, 1996]. ADD-87 protein is present… 

Domains of the Pavarotti kinesin-like protein that direct its subcellular distribution: effects of mislocalisation on the tubulin and actin cytoskeleton during Drosophila oogenesis.

Whether disruption of actin structures by full-length cytoplasmic forms of Pav-KLP is a consequence of the resulting stabilised cytopLasmic microtubules per se or accumulation of the motor protein at ectopic cortical sites to sequester molecules that regulate actin behaviour is discussed.

Different 3' untranslated regions target alternatively processed hu-li tai shao (hts) transcripts to distinct cytoplasmic locations during Drosophila oogenesis.

This work reports here a novel mechanism for localization of transcripts encoding distinct protein isoforms to different destinations in the Drosophila ovary by introducing distinct 3' untranslated regions (3'UTRs) that differentially localize the mRNAs.

Requirement of RBP9, a Drosophila Hu Homolog, for Regulation of Cystocyte Differentiation and Oocyte Determination during Oogenesis

It is shown that RBP9 is expressed not only in the nuclei of neuronal cells but also in the cytoplasm of cystocytes during oogenesis, which suggests that the concentrated localization ofRBP9 protein in the oocyte of the early egg chambers may be required for proper oocyte determination or positioning.

RNA localization in development.

This review considers RNA localization in the context of animal development with a focus on mRNAs and non-protein-coding RNAs localized in Drosophila, Xenopus, ascidian, zebrafish, and echinoderm oocytes and embryos.

The Drosophila wispy gene is required for RNA localization and other microtubule-based events of meiosis and early embryogenesis.

It is shown that wispy is required to recruit or maintain known centrosomal proteins with two types of microtubule organizing centers: the central MTOC that forms between the meiosis II tandem spindles and the centrosomes of the mitotic spindle.

Hts, the Drosophila homologue of adducin, physically interacts with the transmembrane receptor golden goal to guide photoreceptor axons

Hts, the Drosophila homologue of Adducin, physically interacts with Gogo's cytoplasmic domain via its head‐neck domain, thereby guiding R axons in growth cone filopodia.

Eukaryotic translation initiation factor eIF4E-5 is required for spermiogenesis in Drosophila melanogaster

The testis-enriched translation initiation factor eIF4E-5 is needed for spermatid cyst polarization, individualization of mature sperm and male fertility in Drosophila.

Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues.

This review deals with the molecular physiology of spectrin, ankyrin, which links spectrin to the anion exchanger, and two spectrin-associated proteins that promote spectrin interactions with actin: adducin and protein 4.1.

Coordinating the cytoskeleton and endocytosis for regulated plasma membrane growth in the early Drosophila embryo

How plasma membranes are formed around individual nuclei of the syncytial Drosophila embryo provides a model for understanding how cytoskeletal-endocytic cross-talk regulates the assembly of a cell.



Differential distributions of two adducin-like protein isoforms in the Drosophila ovary and early embryo

Adducin co-localises with F-actin and spectrin in the cortex of the oocyte through stage 10 of oogenesis, consistent with a possible role in cytoskeletal assembly or function predicted by mammalian studies.

Different genetic requirements for anterior RNA localization revealed by the distribution of Adducin-like transcripts during Drosophila oogenesis.

A comparison of the spatial distribution of bicoid and Adducin-like transcripts in the maternal-effect RNA-localization mutants exuperantia, swallow, and staufen indicates different genetic requirements for proper localization of these two mRNAs to the anterior pole of the oocyte and early embryo.

Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding

A putative role for adducin is identified, and a calcium- and calmodulin-dependent mechanism whereby higher states of actin association and its interaction with spectrin in the erythrocyte may be controlled is defined.

Primary structure and domain organization of human alpha and beta adducin

The complete sequence of both subunits of human adducin, alpha (737 amino acids), and beta (726 amino acids) has been deduced by analysis of the cDNAs, suggesting evolution by gene duplication.

hu-li tai shao, a gene required for ring canal formation during Drosophila oogenesis, encodes a homolog of adducin.

Drosophila females bearing mutations in a previously undescribed gene, hu-li tai shao [(hts) too little nursing], produced egg chambers that contained fewer than the normal 15 nurse cells and that usually lacked an oocyte, and the hts locus was found to encode a homolog of the mammalian membrane skeletal protein adducin.

Modulation of spectrin–actin assembly by erythrocyte adducin

It is demonstrated that a membrane-skeleton-associated calmodulin-binding protein of erythrocytes, called adducin, binds tightly in vitro to spectrin-actin complexes but with much less affinity either toSpectrin or to actin alone, and is inhibited in its ability to induce the binding of additional spectrin molecules toActin by micromolar concentrations of cal modulin and Ca2+.

How an actin network might cause fountain streaming and nuclear migration in the syncytial Drosophila embryo [published erratum appears in J Cell Biol 1995 Sep;130(5):1231-4]

It is shown here using time-lapse video tapes that cytoplasmic streaming causes nuclear migration along the anterior-posterior axis (axial expansion) in the early syncytial embryo of Drosophila melanogaster, and a working hypothesis for axial expansion based on solation-contraction coupling within the actin network is proposed.

Morphogenesis of Drosophila ovarian ring canals.

The use of antibody reagents to analyze the structure of wild-type and mutant ring canals has shown that ring canal development is a dynamic process of cytoskeletal protein assembly, possibly regulated by tyrosine phosphorylation of some ring canal components.