Rab35 Controls Actin Bundling by Recruiting Fascin as an Effector Protein
Jun Zhang,1
Marko Fonovic,2,3
Kaye Suyama,1
Matthew Bogyo,2
Matthew P. Scott1,*
Actin filaments are key components of the eukaryotic cytoskeleton
that provide mechanical structure and generate forces during
cell shape changes, growth, and migration. Actin filaments are
dynamically assembled into higher-order structures at specified
locations to regulate diverse functions. The Rab family of small
guanosine triphosphatases is evolutionarily conserved and mediates
intracellular vesicle trafficking. We found that Rab35 regulates
the assembly of actin filaments during bristle development in
Drosophila and filopodia formation in cultured cells. These
effects were mediated by the actin-bundling protein fascin,
which directly associated with active Rab35. Targeting Rab35
to the outer mitochondrial membrane triggered actin recruitment,
demonstrating a role for an intracellular trafficking protein
in localized actin assembly.
2 Department of Pathology and Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.
3 Department of Biochemistry, Molecular and Structural Biology, Jozef Stefan Institute, Jamova ulica 39, 1000 Ljubljana, Slovenia.
* To whom correspondence should be addressed. E-mail: mscott{at}stanford.edu
