The multiplicity of human formins: Expression patterns in cells and tissues

• Published in: Cytoskeleton (Hoboken, N.J.) N.J.), 2013-08, Vol.70 (8), p.424-438
• Main Authors: Krainer, Elisabeth C., Ouderkirk, Jessica L., Miller, Eric W., Miller, Matthew R., Mersich, Akos T., Blystone, Scott D.
• Format: Article
• Language: English
• Subjects: actin; actin; tissues; PCR; expression; Actins - metabolism; Adaptor Proteins, Signal Transducing - metabolism; Cytoskeletal Proteins - metabolism; expression; formins; Humans; Intracellular Signaling Peptides and Proteins - metabolism; PCR; Proteins - metabolism; tissues
• ISSN: 1949-3584; 1949-3592
• DOI: 10.1002/cm.21113

Formins are actin‐binding proteins conserved across species from plants to humans. The formin family is defined by their common formin homology (FH2) domains. The 15 distinct human formins are involved in a broad range of cellular functions, including cell adhesion, cytokinesis, cell polarity, and cell morphogenesis. Their commonality is actin polymerization activity inherent to FH2 domains. Although still requiring much study, biochemical activity of formins has been carefully described. In contrast, much less is known of their activities in complex living systems. With the diversity of the formin family and the actin structures that they affect, an extensive future of study beckons. In this study, we report the expression level of all 15 formins in 22 different human cell and tissue types using quantitative real‐time PCR. Identification of major themes in formin expression and documentation of expression profiles should facilitate the cellular study of formins. © 2013 Wiley Periodicals, Inc.