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Sakuno T.,University of Tokyo | Tanaka K.,University of Tokyo | Hauf S.,Friedrich Miescher Laboratory of the Max Planck Society | Watanabe Y.,University of Tokyo
Developmental Cell | Year: 2011

During meiosis I, kinetochores of sister chromatids are juxtaposed or fused and mono-orient, while homologous chromosomes that are paired by chiasmata (bivalents) have to biorient. In the absence of chiasmata, biorientation of sister chromatids (univalents), which carries a risk of aneuploidy, has been occasionally detected in several species, including humans. We show in fission yeast that biorientation of fused sister kinetochores predominates during early prometaphase I. Without chiasmata, this undesirable biorientation of univalents persists and eventually evades the spindle assembly checkpoint, provoking abnormal anaphase. When univalents are connected by chiasmata or by an artificial tether, this erroneous attachment is converted to monopolar attachment and stabilized. This stabilization is apparently achieved by a chromosome configuration that brings kinetochores to the outer edge of the bivalent, while bringing Aurora B, a destabilizer of kinetochore-microtubule attachment, inward. Our results elucidate how chiasmata favor biorientation of bivalents over that of univalents at meiosis I. © 2011 Elsevier Inc.

Hauf S.,Friedrich Miescher Laboratory of the Max Planck Society
Biochemical Society Transactions | Year: 2013

The spindle assembly checkpoint is a conserved mitotic signalling pathway that ensures the equal segregation of chromosomes to daughter cells. Despite intensive work in many model organisms, key features of this safety mechanism remain unexplained. In the present review, I briefly summarize advances made in the last few years, and then focus on unexplored corners of this signalling pathway. © 2013 Biochemical Society.

Chan Y.F.,Friedrich Miescher Laboratory of the Max Planck Society
Current Biology | Year: 2015

How do the legs of jerboas get so long? A comprehensive study of the Dipodidae family of two-legged rodents reveals many evolutionary refinements in toe numbers, bone structures and proportions. Clearly, this adorable emerging developmental model system has legs. © 2015 Elsevier Ltd. All rights reserved.

Antonin W.,Friedrich Miescher Laboratory of the Max Planck Society
Nucleus (Austin, Tex.) | Year: 2011

The inner nuclear membrane (INM) accommodates a specific set of integral membrane proteins many of which interact with chromatin and/or in metazoan cells with the lamina network. The localization of these proteins characterizes this membrane area of the nuclear envelope (NE) despite the fact that the INM forms a membrane continuum with the outer nuclear membrane (ONM) and the remaining endoplasmic reticulum (ER). In fact, the INM can be regarded as a highly specialized membrane subdomain of the ER. How the specific protein composition of the INM is established and maintained and whether this is achieved via a single unifying mechanism is by and large unclear. Recent experiments shed light on some aspects of the process.

Antonin W.,Friedrich Miescher Laboratory of the Max Planck Society
EMBO Journal | Year: 2013

Eukaryotic cells critically rely on a constant and intensive exchange of macromolecules between the cytoplasm and nucleoplasm across the barrier of the nuclear envelope. Nuclear pore complexes (NPCs) function as gates to mediate this transport, but why they grant the selective passage of transport receptor-cargo complexes and at the same time exclude most other cellular macromolecules is incompletely understood. In this issue of The EMBO Journal, Labokha et al (2013) extend our view on how certain NPC proteins form a sieve-like meshwork within the pore that is crucial for these functions. © 2013 European Molecular Biology Organization.

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