Rap1A is a small G protein implicated in a spectrum of biological processes such as cell proliferation, adhesion, differentiation, and embryogenesis. The downstream effectors through which Rap1A mediates its diverse effects are largely unknown. Here we show that Rap1A, but not the related small G proteins Rap2 or Ras, binds the tumor suppressor Ras association domain family 1A (RASSF1A) in a manner that is regulated by phosphorylation of RASSF1A. Interaction with Rap1A is shown to influence the effect of RASSF1A on microtubule behavior.
Amino Acid Sequence ; Animals ; COS Cells ; Cercopithecus aethiops ; HEK293 Cells ; Humans ; Intracellular Space ; metabolism ; Microtubules ; metabolism ; Models, Molecular ; Molecular Sequence Data ; Phosphorylation ; Protein Binding ; Protein Structure, Secondary ; Substrate Specificity ; Tumor Suppressor Proteins ; chemistry ; metabolism ; rap1 GTP-Binding Proteins ; metabolism