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WHAMMing into the Golgi

Garret L Hayes1, Suzanne R Pfeffer

  • 1Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA.

Developmental Cell
|August 13, 2008
PubMed

Insights

Researchers identified WHAMM, a protein that promotes actin polymerization and organizes microtubules, impacting Golgi complex structure and function. This discovery highlights the cytoskeleton

Area of Science:

  • Cell biology
  • Cytoskeletal dynamics
  • Secretory pathway organization

Background:

  • The Golgi complex is crucial for protein modification and transport.
  • Cytoskeletal elements like actin and microtubules play roles in organelle positioning and function.
  • Actin nucleation-promoting factors regulate actin dynamics.

Purpose of the Study:

  • To identify novel proteins involved in Golgi complex organization.
  • To elucidate the role of WHAMM in cytoskeletal regulation and secretory pathway function.

Main Methods:

  • Protein identification and characterization.
  • Biochemical assays for actin polymerization and microtubule binding.
  • Cellular imaging to assess WHAMM localization and Golgi structure.

Main Results:

  • WHAMM (Waste Hexagonal And Microtubule-associated protein) was identified as a multifunctional protein.
  • WHAMM stimulates Arp2/3-mediated actin polymerization.
  • WHAMM binds and organizes microtubules and influences Golgi complex structure and efficiency.
  • WHAMM localizes to the Golgi complex entry face, a novel finding for actin nucleation-promoting factors.

Conclusions:

  • WHAMM is a key regulator linking actin dynamics and microtubule organization to Golgi complex function.
  • The localization of WHAMM highlights the critical role of the cytoskeleton in organizing the secretory pathway.

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