title: Biochemical and functional significance of F-BAR domain proteins interaction with WASP/N-WASP.
abstract: The Bin-Amphiphysin-Rvs (BAR) domain family of proteins includes groups which promote positive (classical BAR, N-BAR, and F-BAR) and negative (I-BAR) membrane deformation. Of these groups, the F-BAR subfamily is the most diverse in its biochemical properties. F-BAR domain proteins dimerize to form a tight scaffold about the membrane. The F-BAR domain provides a banana-shaped, alpha-helical structure that senses membrane curvature. Different types of F-BAR domain proteins contain tyrosine kinase or GTPase activities; some interact with phosphatases and RhoGTPases. Most possess an SH3 domain that facilitates the recruitment and activation of WASP/N-WASP. Thus, F-BAR domain proteins affect remodeling of both membrane and the actin cytoskeleton. The purpose of this review is to highlight the role of F-BAR proteins in coupling WASP/N-WASP to cytoskeletal remodeling. A role for F-BAR/WASP interaction in human diseases affecting nervous, blood, and neoplastic tissues is discussed.
authors: Department of Pediatrics, Northwestern University Feinberg School of Medicine, United States.
authors: Yolande
authors: Y
authors: Chen
authors: Jorie
authors: J
authors: Aardema
authors: Seth J
authors: SJ
authors: Corey
mesh_terms: D000199:Actins / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism*; D006801:Humans; D054730:Protein Interaction Domains and Motifs; D051316:Wiskott-Aldrich Syndrome Protein / Q000378:metabolism*; D051317:Wiskott-Aldrich Syndrome Protein, Neuronal / Q000378:metabolism*
chemical_list: D000199:Actins; D051316:Wiskott-Aldrich Syndrome Protein; D051317:Wiskott-Aldrich Syndrome Protein, Neuronal