4.6 Article

Tropomyosin is an interaction partner of the Drosophila coiled coil protein Yuri Gagarin

Journal

EXPERIMENTAL CELL RESEARCH
Volume 317, Issue 4, Pages 474-487

Publisher

ELSEVIER INC
DOI: 10.1016/j.yexcr.2010.11.012

Keywords

Tropomyosin; Coiled coil proteins; Endoplasmic reticulum; Drosophila; Muscle; Spermatogenesis; Golgins; Actin

Funding

  1. NIH [RO1 HD 39766]
  2. Welch Foundation of Texas [C-1119]
  3. NASA [NNX09AH43G]
  4. NASA [NNX09AH43G, 117920] Funding Source: Federal RePORTER

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The Drosophila gene yuri gagarin is a complex locus encoding three protein isoform classes that are ubiquitously expressed in the organism. Mutations to the gene affect processes as diverse as gravitactic behavior and spermatogenesis. The larger Yuri isoforms contain extensive coiled-coil regions. Our previous studies indicate that one of the large isoform classes (Yuri-65) is required for formation of specialized F-actin-containing structures generated during spermatogenesis, including the so-called actin cones that mediate spermatid individualization. We used the tandem affinity purification of a tagged version of Yuri-65 (the TAP-tagging technique) to identify proteins associated with Yuri-65 in the intact organism. Tropomyosin, primarily as the 284-residue isoform derived from the ubiquitously expressed Tropomyosin 1 gene was thus identified as a major Yuri interaction partner. Co-immunoprecipitation experiments confirmed this interaction. We have established that the stable F-actin cones of spermatogenesis contain Tropomyosin 1 (Tm1) and that in mutant yuri(F64), failure of F-actin cone formation is associated with failure of Tm1 to accumulate at the cone initiation sites. In investigating possible interactions of Tm1 and Yuri in other tissues, we discovered that Tm1 and Yuri frequently colocalize with the endoplasmic reticulum. Tropomyosin has been implicated in actin-mediated membrane trafficking activity in other systems. Our findings suggest that Yuri-Tm1 complexes participate in related functions. (C) 2010 Elsevier Inc. All rights reserved.

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