Publications by authors named "Andrew S Rachlin"
Article Synopsis
- Palladin is a phosphoprotein important for cell adhesion and movement, influencing actin organization when overexpressed.
- It binds to various actin-associated proteins and was shown to directly bind and cross-link actin filaments through specific domains.
- The research suggests that palladin's multiple immunoglobulin (Ig) domains might serve distinct biological roles, potentially aiding in the formation of specialized cell shapes by interacting with actin.
Palladin is a recently described phosphoprotein with an important role in cytoskeletal organization. The major palladin isoform (90-92 kDa) binds to three actin-associated proteins (ezrin, VASP and alpha-actinin), suggesting that palladin functions as a cytoskeletal scaffold. Here, we describe the organization of the palladin gene, which encodes multiple isoforms, including one (140 kDa) with a similar localization pattern to 90 kDa palladin.
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