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Sci. STKE, 20 June 2000
Vol. 2000, Issue 37, p. pe1
[DOI: 10.1126/stke.2000.37.pe1]

PERSPECTIVES

Signal Transduction: Stuck with FYVE Domains

Silvia Corvera

The author is at the Program in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USA. E-mail: silvia.corvera{at}umassmed.edu

Abstract: The FYVE domain is a protein motif that allows the interaction of cytosolic proteins with membranes containing the lipid phosphatidylinositol 3-phosphate. Structural information about FYVE domains has come from two crystal structures and NMR analysis. Corvera discusses how these structures differ and what they tell us about how proteins with FYVE domains interact with biological membranes. The Perspective also addresses how proteins with FYVE domains and protein internalization are involved in signal transduction.

Citation: S. Corvera, Signal Transduction: Stuck with FYVE Domains. Sci. STKE 2000, pe1 (2000).

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