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

@article{Zaccai1996RoleOA,
  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},
  year={1996},
  volume={19 3},
  pages={
          249-57
        }
}
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… 

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References

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

TLDR
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.

TLDR
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

TLDR
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

TLDR
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.

TLDR
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

TLDR
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]

TLDR
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.

TLDR
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.