BRICK 1/HSPC300 functions with SCAR and the ARP2/3 complex to regulate epidermal cell shape in Arabodopsis

Stevan Djakovic, Julia Dyachok, Michael Burke, Mary J. Frank, Laurie G. Smith

Research output: Contribution to journalArticlepeer-review

68 Scopus citations

Abstract

The Arp2/3 complex, a highly conserved nucleator of F-actin polymerization, is essential for a variety of eukaryotic cellular processes, including epidermal cell morphogenesis in Arabidopsis thaliana. Efficient nucleation of actin filaments by the Arp2/3 complex requires the presence of an activator such as a member of the Scar/WAVE family. In mammalian cells, a multiprotein complex consisting of WAVE, PIR121/Sra-1, Nap1, Abi-2 and HSPC300 mediates responsiveness of WAVE to upstream regulators such as Rac. Essential roles in WAVE complex assembly or function have been demonstrated for PIR121/Sra-1, Nap1 and Abi-2, but the significance of HSPC300 in this complex is unclear. Plant homologs of all mammalian WAVE complex components have been identified, including HSPC300, the mammalian homolog of maize BRICK1 (BRK1). We show that, like mutations disrupting the Arabidapsis homologs of PIR121/ Sra-1, Napl and Scar/WAVE, mutations in the Arabidopsis BRK1 gene result in trichome and pavement cell morphology defects (and associated alterations in the F-actin cytoskeleton of expanding cells) similar to those caused by mutations disrupting the ARP2/3 complex itself. Analysis of double mutants provides genetic evidence that BRK1 functions in a pathway with the ARP2/3 complex. BRK1 is required for accumulation of SCAR1 protein in vivo, potentially explaining the apparently essential role of BRK1 in ARP2/3 complex function.

Original languageEnglish (US)
Pages (from-to)1091-1100
Number of pages10
JournalDevelopment
Volume133
Issue number6
DOIs
StatePublished - Mar 2006

Keywords

  • Arp2/3 complex
  • BRICK1
  • HSPC300
  • Pavement cells
  • Trichomes
  • WAVE/Scar

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology

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