A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Molecular Mechanisms of Membrane Deformation by I-BAR Domain Proteins
Tekijät: Saarikangas J, Zhao HX, Pykalainen A, Laurinmaki P, Mattila PK, Kinnunen PKJ, Butcher SJ, Lappalainen P
Kustantaja: CELL PRESS
Julkaisuvuosi: 2009
Journal: Current Biology
Tietokannassa oleva lehden nimi: CURRENT BIOLOGY
Lehden akronyymi: CURR BIOL
Vuosikerta: 19
Numero: 2
Aloitussivu: 95
Lopetussivu: 107
Sivujen määrä: 13
ISSN: 0960-9822
DOI: https://doi.org/10.1016/j.cub.2008.12.029
Tiivistelmä
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.
Ladattava julkaisu This is an electronic reprint of the original article. |  |
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