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Official Journal of the Italian Society of Dermatology and Sexually Transmitted Diseases
Indexed/Abstracted in: EMBASE, PubMed/MEDLINE, Science Citation Index Expanded (SciSearch), Scopus
Impact Factor 1,014
Online ISSN 1827-1820
Byers H. R., Dykstra S.
Department of Dermatology Boston University School of Medicine Boston, MA, USA
Integrins are transmembrane proteins that mediate cell adhesion to the extracellular matrix (ECM). The binding of a subset of integrins to the ECM initiates formation of the focal adhesion, a specialized structural and dynamic signaling linkage with the cytoskeleton. The focal adhesion promotes actin filament assembly and initiates signals regulating cell growth, migration, differentiation and survival. Several regulatory proteins have been characterized at the focal adhesion. Here we review zyxin and its family members as potential candidate regulatory proteins of the focal adhesion. Zyxin, lipoma preferred partner (LPP) and thyroid receptor interacting protein (TRIP6) all localize to focal adhesions via LIM (Lin-1, Isl-1 and Mec-3) domains that act as modular protein-protein binding interfaces. These domains are also found in both proto-oncogene products and transcriptional regulators. Zyxin appears capable of shuttling between the nucleus and focal adhesions. In addition, zyxin shares motifs with listeria ActA protein, which also regulates actin polymerization. These structural and functional characteristics of zyxin and its family members indicate a role in cell signaling and spatial control of actin filament assembly. Recent evidence for zyxin or zyxin-related protein family members in cell migration, proliferation and differentiation is reviewed with emphasis on evidence implicating their role in wound healing, angiogenesis and the development of various benign and malignant tumors including lipoma and melanoma.