Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 378, Issue 5, Pages 976-986Publisher
ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2008.03.014
Keywords
membrane protein; cell adhesion; platelets; image processing; lipid vesicle
Categories
Funding
- NIGMS NIH HHS [U54 GM064346-02S19003, U54 GM064346-019003, U54 GM064346, U54 GM064346-079023, U54 GM064346-029003, U54 GM64346, U54 GM064346-069023] Funding Source: Medline
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Integrins perform the critical function of signalling cell attachment to the extracellular matrix or to other cells. This signalling is done through a structural change propagated bidirectionally across the plasma membrane. Integrin activation has been extensively studied with ectodomain constructs, but the structural change within intact, membrane-bound molecules remains a subject of live debate. Using cryoelectron tomography, we examined the simplest predication of the different integrin activation models, i.e., the change in height of the molecules. Analysis using techniques that compensate for the missing wedge during alignment and averaging and that search for patterns in the structure of the aligned molecular subvolumes extracted from the tomogram reveals that the vast majority of molecules show no dramatic height change upon Mn2+-induced activation of membrane-bound integrins when compared with an inactive integrin control group. Thus, the result is inconsistent with the switchblade activation model. (C) 2008 Elsevier Ltd. All rights reserved.
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