A1 Refereed original research article in a scientific journal
Molecular Mechanisms of Membrane Deformation by I-BAR Domain Proteins
Authors: Saarikangas J, Zhao HX, Pykalainen A, Laurinmaki P, Mattila PK, Kinnunen PKJ, Butcher SJ, Lappalainen P
Publisher: CELL PRESS
Publication year: 2009
Journal: Current Biology
Journal name in source: CURRENT BIOLOGY
Journal acronym: CURR BIOL
Volume: 19
Issue: 2
First page : 95
Last page: 107
Number of pages: 13
ISSN: 0960-9822
DOI: https://doi.org/10.1016/j.cub.2008.12.029
Abstract
Conclusions: These data define I-BAR domain as a functional member of the BAR domain superfamily and unravel the mechanisms by which I-BAR domains deform membranes to induce filopodia in cells. Furthermore, our work reveals unexpected divergence in the mechanisms by which evolutionarily distinct groups of I-BAR domains interact with PI(4,5)P(2)-rich membranes.
Conclusions: These data define I-BAR domain as a functional member of the BAR domain superfamily and unravel the mechanisms by which I-BAR domains deform membranes to induce filopodia in cells. Furthermore, our work reveals unexpected divergence in the mechanisms by which evolutionarily distinct groups of I-BAR domains interact with PI(4,5)P(2)-rich membranes.
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