Critical Reviews™ in Oncogenesis

ISSN for PRINT: 0893-9675

For Online Access

Best Paper Award Selection - Editorial Board Site

2000, Volume11

Issue 1

102 pages

Issue price - $100.00

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, MD, PhD
Associate Professor of Medicine, Section of Hematology/Oncology, Department of Medicine, Pritzker School of Medicine, University of Chicago; Dana-Farber Cancer Institute, Department of Adult Oncology and Division of Medicine, Brigham and Women's Hospital

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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