Literature DB >> 17215303

The Ovhts polyprotein is cleaved to produce fusome and ring canal proteins required for Drosophila oogenesis.

Lisa N Petrella1, Tracy Smith-Leiker, Lynn Cooley.   

Abstract

An essential component of normal development is controlling the transition from cell proliferation to differentiation. One such transition occurs during Drosophila oogenesis. In early oogenesis, germ cells undergo mitotic proliferation and contain a specialized organelle called a fusome, whereas later post-mitotic cells differentiate and lose the fusome as F-actin-rich ring canals form. The hts gene encodes the only Drosophila Adducin, and is a female-sterile mutant that affects both the fusome and ring canals. We show that one Hts protein, Ovhts, is a polyprotein that is cleaved to produce two products, Ovhts-Fus and Ovhts-RC. Whereas Ovhts-Fus localizes to the fusome in mitotic cells, Ovhts-RC localizes to ring canals throughout later oogenesis. We demonstrate that an uncleavable version of Ovhts delays the transition from fusome-containing cells to those that have ring canals. Ovhts is the first polyprotein shown to produce proteins that function in separate structures.

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Year:  2007        PMID: 17215303     DOI: 10.1242/dev.02766

Source DB:  PubMed          Journal:  Development        ISSN: 0950-1991            Impact factor:   6.868


  61 in total

1.  Intercellular protein movement in syncytial Drosophila follicle cells.

Authors:  Stephanie J Airoldi; Peter F McLean; Yuko Shimada; Lynn Cooley
Journal:  J Cell Sci       Date:  2011-12-01       Impact factor: 5.285

Review 2.  The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life.

Authors:  Anthony J Baines
Journal:  Protoplasma       Date:  2010-07-29       Impact factor: 3.356

3.  A Wolbachia nuclease and its binding partner provide a distinct mechanism for cytoplasmic incompatibility.

Authors:  Hongli Chen; Judith A Ronau; John F Beckmann; Mark Hochstrasser
Journal:  Proc Natl Acad Sci U S A       Date:  2019-10-15       Impact factor: 11.205

4.  Detection of in situ protein-protein complexes at the Drosophila larval neuromuscular junction using proximity ligation assay.

Authors:  Simon Wang; SooHyun Yoo; Hae-Yoon Kim; Mannan Wang; Clare Zheng; Wade Parkhouse; Charles Krieger; Nicholas Harden
Journal:  J Vis Exp       Date:  2015-01-20       Impact factor: 1.355

5.  Proximity labeling reveals novel interactomes in live Drosophila tissue.

Authors:  Katelynn M Mannix; Rebecca M Starble; Ronit S Kaufman; Lynn Cooley
Journal:  Development       Date:  2019-07-18       Impact factor: 6.868

6.  Targeted substrate degradation by Kelch controls the actin cytoskeleton during ring canal expansion.

Authors:  Andrew M Hudson; Katelynn M Mannix; Julianne A Gerdes; Molly C Kottemann; Lynn Cooley
Journal:  Development       Date:  2019-01-02       Impact factor: 6.868

7.  Reversible response of protein localization and microtubule organization to nutrient stress during Drosophila early oogenesis.

Authors:  Yuko Shimada; K Mahala Burn; Ryusuke Niwa; Lynn Cooley
Journal:  Dev Biol       Date:  2011-04-23       Impact factor: 3.582

Review 8.  Methods for studying oogenesis.

Authors:  Andrew M Hudson; Lynn Cooley
Journal:  Methods       Date:  2014-01-17       Impact factor: 3.608

9.  HtsRC-Mediated Accumulation of F-Actin Regulates Ring Canal Size During Drosophila melanogaster Oogenesis.

Authors:  Julianne A Gerdes; Katelynn M Mannix; Andrew M Hudson; Lynn Cooley
Journal:  Genetics       Date:  2020-09-03       Impact factor: 4.562

10.  Drosophila Kelch functions with Cullin-3 to organize the ring canal actin cytoskeleton.

Authors:  Andrew M Hudson; Lynn Cooley
Journal:  J Cell Biol       Date:  2010-01-11       Impact factor: 10.539

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