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Critical Reviews™ in Oncogenesis
SJR: 0.631 SNIP: 0.503 CiteScore™: 2.2

ISSN Print: 0893-9675
ISSN Online: 2162-6448

Critical Reviews™ in Oncogenesis

DOI: 10.1615/CritRevOncog.v11.i1.30
14 pages

Role of the Cytoskeletal Protein Paxillin in Oncogenesis

Martin Sattler
Dana-Farber Cancer Institute, Department of Adult Oncology and Division of Medicine, Brigham and Women's Hospital
Evan Pisick
Dana-Farber Cancer Institute, Department of Adult Oncology and Division of Medicine, Brigham and Women's Hospital
Paul T. Morrison
Dana-Farber Cancer Institute, Molecular Biology Core Facilities, Harvard Medical School, 44 Binney Street, Boston, MA 02115
Ravi Salgia
Department of Medical Oncology and Therapeutics Research, Comprehensive Cancer Center, City of Hope National Medical Center


The focal adhesion is an important cellular structure that is involved in cell signaling, cell motility, and oncogenic transformation. Paxillin is a unique adapter protein that is localized to the focal adhesion and is involved in regulating various functions of the focal adhesion. The predicted amino acid structure for paxillin shows at the amino-terminus five LD motifs, a proline-rich domain, several potential phosphorylation sites and four carboxy-terminal LIM domains. Paxillin interacts with cell surface receptors and the actin cytoskeleton and activates several signal transduction pathways that are known to regulate normal cell physiology. Because paxillin is a central protein within the focal adhesion, it is a common target of many different oncoproteins, such as BCR/ABL, v-Src, and E6. In this review we summarize the current knowledge about the structure/function of paxillin and its family members, its role in integrin, cytokine signaling, and oncogenic transformation.

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