SnapShot: Formins

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SnapShot: Formins

See online version for legend and references. Autosomal-dominant nonsyndromic deafness (DFNA1), myeloproliferative defects, defects in T lymphocyte traffi cking and proliferation, tumor cell invasion, defects in natural killer lymphocyte function DIAPH2 (mDia3) Cdc42 Kinetochore Stable microtubule attachment to kinetochore for chromosome alignment Premature ovarian failure DIAPH3 (mDia2) Increa...

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Formins at a glance.

Formins are conserved actin polymerization machines that have instrumental roles in controlling rearrangements of the actin cytoskeleton and have recently been shown to directly regulate microtubule dynamics. Here, and on the accompanying poster, we aim to organize a rapidly expanding body of literature on this diverse protein family, summarizing the common properties that apply to most formins...

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Linking formins to Arp2/3

In This Issue In This Issue Wnt separate ways, met later embers of the Wnt family of secreted signaling proteins control a wide range of developmental and pathological processes, with each Wnt protein signaling through either the " canonical " or " noncanonical " pathway. Two papers in this issue (and a Comment on page 753) now bring these two pathways together, showing that the noncanonical ca...

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Formins as effector proteins of Rho GTPases

Formin proteins were recognized as effectors of Rho GTPases some 15 years ago. They contribute to different cellular actin cytoskeleton structures by their ability to polymerize straight actin filaments at the barbed end. While not all formins necessarily interact with Rho GTPases, a subgroup of mammalian formins, termed Diaphanous-related formins or DRFs, were shown to be activated by small GT...

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Microtubule Stabilization: Formins Assert Their Independence

Mammalian Diaphanous-related (mDia) formins are well known for their actin nucleation and filament elongation activities. They have since emerged as microtubule-binding proteins, and a recent study shows that mDia2 stabilizes microtubules independently of its actin nucleation activity.

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ژورنال

عنوان ژورنال: Cell

سال: 2010

ISSN: 0092-8674

DOI: 10.1016/j.cell.2010.06.030