Abstract:
:In mammalian oocytes, three actin binding proteins, Formin 2 (Fmn2), Spire, and profilin, synergistically organize a dynamic cytoplasmic actin meshwork that mediates translocation of the spindle toward the cortex and is required for successful fertilization. Here we characterize Fmn2 and elucidate the molecular mechanism for this synergy, using bulk solution and individual filament kinetic measurements of actin assembly dynamics. We show that by capping filament barbed ends, Spire recruits Fmn2 and facilitates its association with barbed ends, followed by rapid processive assembly and release of Spire. In the presence of actin, profilin, Spire, and Fmn2, filaments display alternating phases of rapid processive assembly and arrested growth, driven by a "ping-pong" mechanism, in which Spire and Fmn2 alternately kick off each other from the barbed ends. The results are validated by the effects of injection of Spire, Fmn2, and their interacting moieties in mouse oocytes. This original mechanism of regulation of a Rho-GTPase-independent formin, recruited by Spire at Rab11a-positive vesicles, supports a model for modulation of a dynamic actin-vesicle meshwork in the oocyte at the origin of asymmetric positioning of the meiotic spindle.
journal_name
PLoS Bioljournal_title
PLoS biologyauthors
Montaville P,Jégou A,Pernier J,Compper C,Guichard B,Mogessie B,Schuh M,Romet-Lemonne G,Carlier MFdoi
10.1371/journal.pbio.1001795subject
Has Abstractpub_date
2014-02-25 00:00:00pages
e1001795issue
2eissn
1544-9173issn
1545-7885pii
PBIOLOGY-D-13-03073journal_volume
12pub_type
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