Shortstop recruits EB1/APC1 and promotes microtubule assembly at the muscle-tendon junction

Research output: Contribution to journalArticle

  • External authors:
  • Arul Subramanian
  • Misato Yamamoto
  • Kaoru Sugimura
  • Tadashi Uemura
  • Joerg Betschinger
  • Juergen A. Knoblich
  • Talila Volk

Abstract

Background: Shot (previously named Kakapo), is a Drosophila Plakin family member containing both Actin binding and microtubule binding domains. In Drosophila, it is required for a wide range of processes, including axon extension, dendrite formation, axonal terminal arborization at the neuromuscular junction, tendon cell development, and adhesion of wing epithelium. Results: To address how Shot exerts its activity at the molecular level, we investigated the molecular interactions of Shot with candidate proteins in mature larval tendon cells. We show that Shot colocalizes with EB1/APC1 and with a compact microtubule array extending between the muscle-tendon junction and the cuticle. Shot forms a protein complex with EB1 via its C-terminal EF-hands and GAS2-containing domains. In tendon cells with reduced Shot activity, EB1/APC1 dissociate from the muscle-tendon junction, and the microtubule array elongates. The resulting tendon cell, although associated with the muscle and the cuticle ends, loses its stress resistance and elongates. Conclusions: Our results suggest that Shot mediates tendon stress resistance by the organization of a compact microtubule network at the muscle-tendon junction. This is achieved by Shot association with the cytoplasmic faces of the basal hemiadherens junction and with the EB1/APC1 complex.

Bibliographical metadata

Original languageEnglish
Pages (from-to)1086-1095
Number of pages9
JournalCurrent Biology
Volume13
Issue number13
DOIs
Publication statusPublished - 1 Jul 2003