Osmotic stress-induced remodeling of the cortical cytoskeleton

Caterina Di Ciano, Zilin Nie, Katalin Szászi, Alison Lewis, Takehito Uruno, Xi Zhan, Ori D. Rotstein, Alan Mak, András Kapus

Research output: Contribution to journalArticle

117 Citations (Scopus)

Abstract

Osmotic stress is known to affect the cytoskeleton; however, this adaptive response has remained poorly characterized, and the underlying signaling pathways are unexplored. Here we show that hypertonicity induces submembranous de novo F-actin assembly concomitant with the peripheral translocation and colocalization of cortactin and the actin-related protein 2/3 (Arp2/3) complex, which are key components of the actin nucleation machinery. Additionally, hyperosmolarity promotes the association of cortactin with Arp2/3 as revealed by coimmunoprecipitation. Using various truncation or phosphorylation-incompetent mutants, we show that cortactin translocation requires the Arp2/3- or the F-actin binding domain, but the process is independent of the shrinkage-induced tyrosine phosphorylation of cortactin. Looking for an alternative signaling mechanism, we found that hypertonicity stimulates Rac and Cdc42. This appears to be a key event in the osmotically triggered cytoskeletal reorganization, because 1) constitutively active small GTPases translocate cortactin, 2) Rac and cortactin colocalize at the periphery of hypertonically challenged cells, and 3) dominant-negative Rac and Cdc42 inhibit the hypertonicity-provoked cortactin and Arp3 translocation. The Rho family-dependent cytoskeleton remodeling may be an important osmoprotective response that reinforces the cell cortex.

Original languageEnglish
Pages (from-to)C850-C865
JournalAmerican Journal of Physiology - Cell Physiology
Volume283
Issue number3 52-3
DOIs
Publication statusPublished - Sep 2002
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Physiology
  • Cell Biology

Fingerprint Dive into the research topics of 'Osmotic stress-induced remodeling of the cortical cytoskeleton'. Together they form a unique fingerprint.

Cite this